The world’s most compressed sentence

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The world’s most compressed sentence

All biology, all sciences about science and all evolution of light and frequencies, and all history is compressed and collected in a single DNA strand as the eye can not even see, there our Blueprint is like a super compressed XML.file for quantum computers, and humans need their lighbody to be able to read and understand the Blueprint (RNA/DNA code) – just like computers needs XML – files.

Bildresultat för my kingdom is not of this world

Even if the Swedish Government and science in west world think otherwise

 

Nascent state (chemistry)

Nascent state or in statu nascendi (Lat. newly formed moiety: in the state of being born or just emerging), in chemistry, refers to the form of a chemical element (or sometimes compound) in the instance of their liberation or formation. Often encountered are atomic oxygen (Onasc), nascent hydrogen (Hnasc), and similar forms of chlorine (Clnasc) or bromine (Brnasc). The monatomic nascent forms tend to be more reactive than their most common forms.

Serious efforts to understand how proteins are encoded began after the structure of DNA was discovered in 1953. George Gamow postulated that sets of three bases must be employed to encode the 20 standard amino acids used by living cells to build proteins. With four different nucleotides, a code of 2 nucleotides would allow for only a maximum of 42 = 16 amino acids. A code of 3 nucleotides could code for a maximum of 43 = 64 amino acids.

Global flexibility: multiple domains

The presence of multiple domains in proteins gives rise to a great deal of flexibility and mobility, leading to protein domain dynamics.[1] Domain motions can be inferred by comparing different structures of a protein (as in Database of Molecular Motions), or they can be directly observed using spectra.

The changes made in the master cell will be replicated throughout the entire body.

THE MASTER CELL

”Within the pineal glan is what is called the master cell, and it is this cell that is the operation centre fo all other cells int the body. The master cell is the starting point of heling for many of the functions that the body perfoms. Within it is the chromosome f DNA that is teh heart of the DNA activation. Inside the master cell is a tiny universe all its own that is a mastser key to our function. it runs everything in the body, from the colour of our hai to the way we wiggle our feet. All parts of the body are controlled by the programmes in the chromosomes and the DNA. And inside the master cell are the youth and vitality chromosomes.”

Telomere

A telomere is a region of repetitive nucleotide sequences at each end of a chromosome, which protects the end of the chromosome from deterioration or from fusion with neighboring chromosomes. Its name is derived from the Greek nouns telos (τέλος) ‘end’ and merοs (μέρος, root: μερ-) ‘part.’ For vertebrates, the sequence of nucleotides in telomeres is TTAGGG, with the complementary DNA strand being AATCCC

Telomeres are repetitive nucleotide sequences located at the termini of linear chromosomes of most eukaryotic organisms. For vertebrates, the sequence of nucleotides in telomeres is TTAGGG.

https://en.wikipedia.org/wiki/Telomere

Are Telomeres the Key to Aging and Cancer

Inside the nucleus of a cell, our genes are arranged along twisted, double-stranded molecules of DNA called chromosomes. At the ends of the chromosomes are stretches of DNA called telomeres, which protect our genetic data, make it possible for cells to divide, and hold some secrets to how we age and get cancer. So telomeres also have been compared with a bomb fuse.

What do telomeres do?

Telomeres serve three major purposes:

  1. They help to organise each of our 46 chromosomes in the nucleus? (control centre) of our cells?.
  2. They protect the ends of our chromosomes by forming a cap, much like the plastic tip on shoelaces. If the telomeres were not there, our chromosomes may end up sticking to other chromosomes.
  3. They allow the chromosome to be replicated properly during cell division

http://www.yourgenome.org/facts/what-is-a-telomere

 

Nuclear membrane – Human cell nucleus

Diagram human cell nucleus.svg

A nuclear membrane, also known as the [1] nucleolemma[2] or karyotheca,[3] is the phospho lipid bilayer membrane which surrounds the genetic material and nucleolus in eukaryotic cells.

https://en.wikipedia.org/wiki/Nuclear_membrane

If Nature wanted to protect the information contained in the genetic code of a species – would do it

Infogad bild 1

Eukaryote

A eukaryote (/juːˈkæri.t/ or /juːˈkæriət/ yoo-KARR-ee-oht or yoo-KARR-ee-ət) is any organism whose cells contain a nucleus and other organelles enclosed within membranes.

https://en.wikipedia.org/wiki/Eukaryote

Monophyly

n common cladistic usage, a monophyletic group is a taxon (group of organisms) which forms a clade, meaning that it consists of an ancestral species and all its descendants. The term is synonymous with the uncommon term holophyly. Monophyletic groups are typically characterized by shared derived characteristics (synapomorphies).

Monophyly is contrasted with paraphyly and polyphyly

https://en.wikipedia.org/wiki/Monophyly

Clade

A clade (from Ancient Greek: κλάδος, klados, ”branch”) is a group of organisms that consists of a common ancestor and all its lineal descendants, and represents a single ”branch” on the ”tree of life”.

https://en.wikipedia.org/wiki/Clade

Nascent state or in statu nascendi (Lat. newly formed moiety: in the state of being born or just emerging), in chemistry, refers to the form of a chemical element (or sometimes compound) in the instance of their liberation or formation.

Alchemical process – transmutation – monatomic cell – a new state of being born in the molecular evolution. Second birth is a moving from 2 DNA to activate 10 etheric DNA strands. The birth of the lightbody. Other explain is this a movement from 3 dimensional world to a 5 dimensional world in the evolution and new genes evolving.

Monatomic hydrogen comprises about 75% of the elemental mass of the universe.

Hydrogen is a chemical element with chemical symbol H and atomic number 1. With an atomic weight of 1.00794 u, hydrogen is the lightest element on the periodic table. Most of the hydrogen on Earth exists in molecular forms such as water or organic compounds.

Psysical DNA is composed of hydrogen bonds. In chemistry, ahydrogen bond easist bond to change. this means that thought focuses in the correct way can affect DNA.

DNA is very stable in its double-stranded form. For many processes of DNA metabolism, such as replication, repair, recombination and transcription, the DNA has to be brought transiently into a single-stranded form. DNA helicases are enzymes capable of melting the hydrogen bonds of base pairs by using the energy of nucleoside-5′-triphosphate hydrolysis. This minireview focusses on the current knowledge of DNA helicases from eukaryotic cells.

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Eukaryotic cell

Bildresultat för eukaryotic cellsBildresultat för eukaryotic cells

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G4-DNA – Quadruplexes – 4 strand DNA

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3D Structure of the intramolecular human telomeric G-quadruplex in potassium solution (PDB ID 2HY9). The backbone is represented by a tube. The center of this structure contains three layers of G-tetrads. The hydrogen bonds in these layers are represented by blue dashed lines.

Besides double helices and the above-mentioned triplexes, RNA and DNA can both also form quadruple helices. There are diverse structures of RNA base quadruplexes. Four consecutive guanine residues can form a quadruplex in RNA by Hoogsteen hydrogen bonds to form a “Hoogsteen ring” (See Figure).[11] G-C and A-U pairs can also form base quadruplex with a combination of Watson-Crick pairing and noncanonical pairing in the minor groove.[14]

https://en.wikipedia.org/wiki/G-quadruplex

”The genesis of the DNA-unwinding machinery is wonderfully complex and surprising,”

How Helicase Unwinds the DNA Double Helix in Preparation for Replication

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https://pharmaceuticalintelligence.com/2014/07/

Why DNA Helicase is Protein Of The Year!

Many different forms of DNA Helicase exist in the world, with slight differences in structure generally occurring between species of living organisms (shown below). Most of the crystal structures of helicases that have been solved so far have come from small bacteria or yeast, where it’s easiest to isolate the one specific enzyme. But despite these different forms and structures, all forms of DNA Helicase have the same, very important job. It uses the energy from hydrolysis of ATP to break the many hydrogen bonds that form between base pairs of the nucleic acids that make up DNA and keep it held together in its classic double-helical shape.

1CR11Q57

The products of the ”reaction” then are single strands of DNA that have been unzipped and can then be replicated by other enzymes. Humans can developed new protein enzymes when the 2 DNA strand have been unzipped

http://amerwood261.blogspot.se/2011/04/many-different-forms-of-dna-helicase.html

DNA Helicase

DNA helicase pries apart the two strands in a DNA double helix, powered by ATP

 

DNA helicase pulling a single strand of DNA (orange) through the center.

Our genetic information is safely locked up inside the double helix of DNA. In order to use this information, the helix must be unwound to expose the bases, allowing polymerases access to build complementary DNA or RNA strands. Unwinding of DNA is trickier than you might expect. The interaction between bases is quite strong and there are many, many of them, so it takes appreciable energy to separate the strands. This is the job of DNA helicases: they are enzymes that pull apart the two strands in a DNA double helix.

https://pdb101.rcsb.org/motm/168

Protein multifunctionality

Protein multifunctionality may be one of the ways a cell makes more with less.

The proper physical methods are ultracentrifugation, gel filtration, and PAGE in with and without denaturing agents to determine the molecular weight of the native protein and the number of its subunits. Isoelectric focusing may provide indirect evidence that the subunits are identical. The number of autonomous functions must exceed the number of separable protein bands. The protein band must be homogeneous. Final proof is evidently provided by the total sequence of the protein or of the coding gene (cDNA in the case of eukaryotes).

Extreme multifunctional proteins identified from a human protein interaction network

http://www.nature.com/articles/ncomms8412

Protein moonlighting

proteon-moon

Protein moonlighting (or gene sharing) is a phenomenon by which a protein can perform more than one function.[2] Ancestral moonlighting proteins originally possessed a single function but through evolution, acquired additional functions. Many proteins that moonlight are enzymes; others are receptors, ion channels or chaperones. The most common primary function of moonlighting proteins is enzymatic catalysis, but these enzymes have acquired secondary non-enzymatic roles. Some examples of functions of moonlighting proteins secondary to catalysis include signal transduction, transcriptional regulation, apoptosis, motility, and structural.[3]

Protein moonlighting may occur widely in nature. Protein moonlighting through gene sharing differs from the use of a single gene to generate different proteins by alternative RNA splicing, DNA rearrangement, or post-translational processing. It is also different from multifunctionality of the protein, in which the protein has multiple domains, each serving a different function. Protein moonlighting by gene sharing means that a gene may acquire and maintain a second function without gene duplication and without loss of the primary function. Such genes are under two or more entirely different selective constraints.[4]

Various techniques have been used to reveal moonlighting functions in proteins. The detection of a protein in unexpected locations within cells, cell types, or tissues may suggest that a protein has a moonlighting function. Furthermore, sequence or structure homology of a protein may be used to infer both primary function as well as secondary moonlighting functions of a protein.

https://en.wikipedia.org/wiki/Protein_moonlighting

Crystallins

crysatallin

The most well-studied examples of gene sharing are crystallins. These proteins, when expressed at low levels in many tissues function as enzymes, but when expressed at high levels in eye tissue, become densely packed and thus form lenses.

In the case of crystallins, the genes must maintain sequences for catalytic function and transparency maintenance function.[4] The abundant lens crystallins have been generally viewed as static proteins serving a strictly structural role in transparency and cataract

Alpha crystallins

Alpha-crystallin B chain is a protein that in humans is encoded by the CRYAB gene

https://en.wikipedia.org/wiki/CRYAB

Beta/gamma-crystallins

Corneal crystallins

https://en.wikipedia.org/wiki/Homology_(mathematics)

https://en.wikipedia.org/wiki/Euler_characteristic

polyhydron

quadrilateral polyhedron

A polyhedron is a 3-dimensional example of the more general polytope in any number of dimensions

https://en.wikipedia.org/wiki/Polyhedron

https://en.wikipedia.org/wiki/Topological_space

 

Nucleic acid tertiary structure

https://en.wikipedia.org/wiki/Nucleic_acid_tertiary_structure

The WRN gene

The WRN gene is located on the short (p) arm of chromosome 8 between positions 12 and 11.2, from base pair 31,010,319 to base pair 31,150,818.

DNA helicase, RecQ-like type 3 is an enzyme that in humans is encoded by the WRN gene. WRN is a member of the RecQ Helicase family.[3] Helicase enzymes generally unwind and separate double-stranded DNA. These activities are necessary before DNA can be copied in preparation for cell division (DNA replication). Helicase enzymes are also critical for making a blueprint of a gene for protein production, a process called transcription. Further evidence suggests that Werner protein plays a critical role in repairing DNA. Overall, this protein helps maintain the structure and integrity of a person’s DNA.

WRN is an oligomer that can act as a monomer when unwinding DNA, but as a dimer in solution or a tetramer when complexed with DNA, and has also been observed in tetrameric and hexameric forms.

WRN is a helicase and exonuclease involved in many DNA repair and processing pathways [1265]. Genetic variation studies in breast cancer patients, showed that WRN might have an important tumorigenic role [3648]. Its exact functions remain unknown, but it is one of the strongest candidates for genes influencing human ageing.

http://genomics.senescence.info/genes/entry.php?hgnc=WRN

Helicase enzymes

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Helicases are a class of enzymes vital to all living organisms. Their main function is to unpackage an organism’s genes. They are motor proteins that move directionally along a nucleic acid phosphodiester backbone, separating two annealed nucleic acid strands (i.e., DNA, RNA, or RNA-DNA hybrid) using energy derived from ATP hydrolysis. There are many helicases resulting from the great variety of processes in which strand separation must be catalyzed. Approximately 1% of eukaryotic genes code for helicases.[1]

The human genome codes for 95 non-redundant helicases: 64 RNA helicases and 31 DNA helicases.[2] Many cellular processes, such as DNA replication, transcription, translation, recombination, DNA repair, and ribosome biogenesis involve the separation of nucleic acid strands.

RNA helicases are essential for most processes of RNA metabolism such as ribosome biogenesis, pre-mRNA splicing, and translation initiation. They also play an important role in sensing viral RNAs.[51] RNA helicases are involved in the mediation of antiviral immune response because they can identify foreign RNAs in vertebrates. About 80% of all viruses are RNA viruses and they contain their own RNA helicases.

https://en.wikipedia.org/wiki/Helicase

What is the role of DNA helicase, DNA polymerase and DNA ligase in DNA replication? Are all of them equally important?

DNA helicase unwinds DNA, ready for transcription

DNA polymerase allows the replication of identical strands of DNA

DNA ligase joins strands of DNA back together

https://www.quora.com/What-is-the-role-of-DNA-helicase-DNA-polymerase-and-DNA-ligase-in-DNA-replication-Are-all-of-them-equally-important

Helicase enzymes Superfamilies

Helicases are classified in 6 groups (superfamilies) based on their shared sequence motifs.[24] Helicases not forming a ring structure are in superfamilies 1 and 2, and ring-forming helicases form part of superfamilies 3 to 6.[25] Helicases are also classified as α or β depending on if they work with single or double-strand DNA; α helicases work with single-strand DNA and β helicases work with double-strand DNA. They are also classified by translocation polarity. If translocation occurs 3’-5’ the helicase is type A; if translocation occurs 5’-3’ it is type B.[24]

  • Superfamily 1 (SF1): This superfamily can be further subdivided into SF1A and SF1B helicases.[24] In this group helicases can have either 3’-5’ (SF1A subfamily) or 5’-3’(SF1B subfamily) translocation polarity.[24][26] The most known SF1A helicases are Rep and UvrD in gram-negative bacteria and PcrA helicase from gram-positive bacteria.[24] The most known Helicases in the SF1B group are RecD and Dda helicases.[24]
  • Superfamily 2 (SF2): This is the largest group of helicases that are involved in varied cellular processes.[24][27] They are characterized by the presence of nine conserved motifs: Q, I, Ia, Ib, and II through VI.[27] This group is mainly composed of DEAD-box RNA helicases.[25] Some other helicases included in SF2 are the RecQ-like family and the Snf2-like enzymes.[24] Most of the SF2 helicases are type A with a few exceptions such as the XPD family.[24]
  • Superfamily 3 (SF3): Superfamily 3 consists of helicases encoded mainly by small DNA viruses and some large nucleocytoplasmic DNA viruses.[28][29] They have a 3’-5’ translocation directionality, meaning that they are all type A helicases.[24] The most known SF3 helicase is the papilloma virus E1 helicase.[24]
  • Superfamily 4 (SF4): All SF4 family helicases have a type B polarity (5’-3’).[24] The most studied SF4 helicase is gp4 from bacteriophage T7.[24]
  • Superfamily 5 (SF5): Rho proteins conform the SF5 group.[24]
  • Superfamily 6 (SF6): They contain the core AAA+ that is not included in the SF3 classification.[24] Some proteins in the SF6 group are: mini chromosome maintenance MCM, RuvB, RuvA, and RuvC.[24]

Sequence motif

In genetics, a sequence motif is a nucleotide or amino-acid sequence pattern that is widespread and has, or is conjectured to have, a biological significance. For proteins, a sequence motif is distinguished from a structural motif, a motif formed by the three-dimensional arrangement of amino acids which may not be adjacent.

An example is the N-glycosylation site motif:

Asn, followed by anything but Pro, followed by either Ser or Thr, followed by anything but Pro

where the three-letter abbreviations are the conventional designations for amino acids (see genetic code).

https://en.wikipedia.org/wiki/Sequence_motif

 

Phosphodiester bond

A phosphodiester bond occurs when exactly two of the hydroxyl groups in phosphoric acid react with hydroxyl groups on other molecules to form two ester bonds.[1]

Phosphodiester bonds are central to all life on Earth,[fn 1] as they make up the backbone of the strands of nucleic acid. In DNA and RNA, the phosphodiester bond is the linkage between the 3′ carbon atom of one sugar molecule and the 5′ carbon atom of another, deoxyribose in DNA and ribose in RNA. Strong covalent bonds form between the phosphate group and two 5-carbon ring carbohydrates (pentoses) over two ester bonds.

https://en.wikipedia.org/wiki/Phosphodiester_bond

MDA5

MDA5 (Melanoma Differentiation-Associated protein 5) is a RIG-I-like receptor dsRNA helicase enzyme that in humans is encoded by the IFIH1 gene.[4] MDA5 is part of the RIG-I-like receptor (RLR) family, which also includes RIG-I and LGP2, and functions as a pattern recognition receptor (recognizing dsRNA) that is a sensor for viruses.

Motor protein

Motor proteins are class of molecular motors that are able to move along the surface of a suitable substrate. They convert chemical energy into mechanical work by the hydrolysis of ATP. Flagellar rotation, however, is powered by proton pump.

Cellular functions

The best prominent example of a motor protein is the muscle protein myosin which ”motors” the contraction of muscle fibers in animals. Motor proteins are the driving force behind most active transport of proteins and vesicles in the cytoplasm. Kinesins and cytoplasmic dyneins play essential roles in intracellular transport such as axonal transport and in the formation of the spindle apparatus and the separation of the chromosomes during mitosis and meiosis. Axonemal dynein, found in cilia and flagella, is crucial to cell motility, for example in spermatozoa, and fluid transport, for example in trachea.

https://en.wikipedia.org/wiki/Motor_protein

Cytoskeletal motor proteins

Motor proteins utilizing the cytoskeleton for movement fall into two categories based on their substrates: Actin motors such as myosin move along microfilaments through interaction with actin. Microtubule motors such as dynein and kinesin move along microtubules through interaction with tubulin. There are two basic types of microtubule motors: plus-end motors and minus-end motors, depending on the direction in which they ”walk” along the microtubule cables within the cell.

Other molecular motors

Besides the motor proteins above, there are many more types of proteins capable of generating forces and torque in the cell. Many of these molecular motors are ubiquitous in both prokaryotic and eukaryotic cells, although some, such as those involved with cytoskeletal elements or chromatin, are unique to eukaryotes. The motor protein prestin,[13] expressed in mammalian cochlear outer hair cells, produces mechanical amplification in the cochlea. It is a direct voltage-to-force converter, which operates at the microsecond rate and possesses piezoelectric properties.

Cytoskeleton

https://en.wikipedia.org/wiki/Cytoskeleton

Chromatin

https://en.wikipedia.org/wiki/Chromatin

Prestin

https://en.wikipedia.org/wiki/Prestin

Molecular motor

Examples

  • Cytoskeletal motors
    • Myosins are responsible for muscle contraction, intracellular cargo transport, and producing cellular tension.
    • Kinesin moves cargo inside cells away from the nucleus along microtubules.
    • Dynein produces the axonemal beating of cilia and flagella and also transports cargo along microtubules towards the cell nucleus.
  • Polymerisation motors
    • Actin polymerization generates forces and can be used for propulsion. ATP is used.
    • Microtubule polymerization using GTP.
    • Dynamin is responsible for the separation of clathrin buds from the plasma membrane. GTP is used.
  • Rotary motors:
    • FoF1-ATP synthase family of proteins convert the chemical energy in ATP to the electrochemical potential energy of a proton gradient across a membrane or the other way around. The catalysis of the chemical reaction and the movement of protons are coupled to each other via the mechanical rotation of parts of the complex. This is involved in ATP synthesis in the mitochondria and chloroplasts as well as in pumping of protons across the vacuolar membrane.[3]
    • The bacterial flagellum responsible for the swimming and tumbling of E. coli and other bacteria acts as a rigid propeller that is powered by a rotary motor. This motor is driven by the flow of protons across a membrane, possibly using a similar mechanism to that found in the Fo motor in ATP synthase.
  • Nucleic acid motors:
    • RNA polymerase transcribes RNA from a DNA template.[4]
    • DNA polymerase turns single-stranded DNA into double-stranded DNA.[5]
    • Helicases separate double strands of nucleic acids prior to transcription or replication. ATP is used.
    • Topoisomerases reduce supercoiling of DNA in the cell. ATP is used.
    • RSC and SWI/SNF complexes remodel chromatin in eukaryotic cells. ATP is used.
    • SMC proteins responsible for chromosome condensation in eukaryotic cells.[6]
    • Viral DNA packaging motors inject viral genomic DNA into capsids as part of their replication cycle, packing it very tightly.[7] Several models have been put forward to explain how the protein generates the force required to drive the DNA into the capsid; for a review, see [1]. An alternative proposal is that, in contrast with all other biological motors, the force is not generated directly by the protein, but by the DNA itself.[8] In this model, ATP hydrolysis is used to drive protein conformational changes that alternatively dehydrate and rehydrate the DNA, cyclically driving it from B-DNA to A-DNA and back again. A-DNA is 23% shorter than B-DNA, and the DNA shrink/expand cycle is coupled to a protein-DNA grip/release cycle to generate the forward motion that propels DNA into the capsid.
  • Synthetic molecular motors have been created by chemists that yield rotation, possibly generating torque.

https://en.wikipedia.org/wiki/Molecular_motor

Golgi apparatus

The Golgi apparatus (/ˈɡl/), also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic cells.[1] It was identified in 1897 by the Italian scientist Camillo Golgi and named after him in 1898.[2]

Part of the cellular endomembrane system, the Golgi apparatus packages proteins into membrane-bound vesicles inside the cell before the vesicles are sent to their destination. The Golgi apparatus resides at the intersection of the secretory, lysosomal, and endocytic pathways. It is of particular importance in processing proteins for secretion, containing a set of glycosylation enzymes that attach various sugar monomers to proteins as the proteins move through the apparatus.

The Golgi apparatus is a major collection and dispatch station of protein products received from the endoplasmic reticulum (ER). Proteins synthesized in the ER are packaged into vesicles, which then fuse with the Golgi apparatus.

https://en.wikipedia.org/wiki/Golgi_apparatus

Oligomer

https://en.wikipedia.org/wiki/Oligomer

Exonuclease

Exonucleases are enzymes that work by cleaving nucleotides one at a time from the end (exo) of a polynucleotide chain. A hydrolyzing reaction that breaks phosphodiester bonds at either the 3’ or the 5’ end occurs. Its close relative is the endonuclease, which cleaves phosphodiester bonds in the middle (endo) of a polynucleotide chain. Eukaryotes and prokaryotes have three types of exonucleases involved in the normal turnover of mRNA: 5’ to 3’ exonuclease, which is a dependent decapping protein; 3’ to 5’ exonuclease, an independent protein; and poly(A)-specific 3’ to 5’ exonuclease.

https://en.wikipedia.org/wiki/Exonuclease

Crystal structure

In crystallography, crystal structure is a description of the ordered arrangement of atoms, ions or molecules in a crystalline material.[3] Ordered structures occur from the intrinsic nature of the constituent particles to form symmetric patterns that repeat along the principal directions of three-dimensional space in matter.

The smallest group of particles in the material that constitutes the repeating pattern is the unit cell of the structure. The unit cell completely defines the symmetry and structure of the entire crystal lattice, which is built up by repetitive translation of the unit cell along its principal axes.

https://en.wikipedia.org/wiki/Crystal_structure

Bravais lattice

In geometry and crystallography, a Bravais lattice, studied by Auguste Bravais (1850),[1] is an infinite array of discrete points in three dimensional space generated by a set of discrete translation operations described by:

Bravais lattices in 2 dimensions

In two-dimensional space, there are 5 Bravais lattices,[2] grouped into four crystal families.

Bravais lattices in 3 dimensions

n three-dimensional space, there are 14 Bravais lattices. These are obtained by combining one of the six crystal families with one of the centering types.

https://en.wikipedia.org/wiki/Bravais_lattice

Mammal

Mammals are any vertebrates within the class Mammalia (/məˈmli.ə/ from Latin mamma ”breast”), a clade of endothermic amniotes distinguished from reptiles and birds by the possession of a neocortex (a region of the brain), hair, three middle ear bones and mammary glands. The sister group of Mammals may be the extinct Haldanodon. The Mammals represent the only living Synapsida, which together with the Sauropsida form the Amniota clade. The Mammals consist of the Australosphenida including monotrema and the theria.

Mammals include the largest animals on the planet, the great whales, as well as some of the most intelligent, such as elephants, primates and cetaceans. The basic body type is a terrestrial quadruped, but some mammals are adapted for life at sea, in the air, in trees, underground or on two legs. The largest group of mammals, the placentals, have a placenta, which enables the feeding of the fetus during gestation. Mammals range in size from the 30–40 mm (1.2–1.6 in) bumblebee bat to the 30-meter (98 ft) blue whale.

In human culture, domesticated mammals played a major role in the Neolithic revolution, causing farming to replace hunting and gathering, and leading to a major restructuring of human societies with the first civilizations. They provided, and continue to provide, power for transport and agriculture, as well as various commodities such as meat, dairy products, wool, and leather. Mammals are hunted or raced for sport, and are used as model organisms in science. Mammals have been depicted in art since Palaeolithic times, and appear in literature, film, mythology, and religion.

https://en.wikipedia.org/wiki/Mammal

Secret to a longer life for humans may lie in the DNA of a whale that lives for 200 years

  • Researchers studied the unique genetic patterns of the bowhead whale
  • The world’s longest-lived mammal with a lifespan of more than 200 years
  • Identified unique genes that help them avoid diseases, including cancer
  • And now scientists wants to use genes to prolong human life 

 

http://www.dailymail.co.uk/news/article-2896374/Secret-longer-life-humans-lie-DNA-whale-lives-200-years.html

Horizontal gene transfer

Horizontal gene transfer (HGT) is the movement of genetic material between unicellular and/or multicellular organisms other than via vertical transmission (the transmission of DNA from parent to offspring.) [1] HGT is synonymous with lateral gene transfer (LGT) and the terms are interchangeable.[2][3][4] HGT has been shown to be an important factor in the evolution of many organisms.

https://en.wikipedia.org/wiki/Horizontal_gene_transfer

Jumping gene

A transposon (jumping gene) is a mobile segment of DNA that can sometimes pick up a resistance gene and insert it into a plasmid or chromosome, thereby inducing horizontal gene transfer of antibiotic resistance.

A transposable element (TE or transposon) is a DNA sequence that can change its position within a genome, sometimes creating or reversing mutations and altering the cell’s genome size. Transposition often results in duplication of the TE. Barbara McClintock‘s discovery of these jumping genes.

Horizontal transposon transfer (HTT) refers to the passage of pieces of DNA that are characterized by their ability to move from one locus to another between genomes by means other than parent-to-offspring inheritance. Horizontal gene transfer has long been thought to be crucial to prokaryotic evolution, but there is a growing amount of data showing that HTT is a common and widespread phenomenon in eukaryote evolution as well.

https://en.wikipedia.org/wiki/Transposable_element

https://en.wikipedia.org/wiki/Mobile_genetic_elements

Horizontal gene transfer is a potential confounding factor in inferring phylogenetic trees based on the sequence of one gene.[91] For example, given two distantly related bacteria that have exchanged a gene a phylogenetic tree including those species will show them to be closely related because that gene is the same even though most other genes are dissimilar. For this reason it is often ideal to use other information to infer robust phylogenies such as the presence or absence of genes or, more commonly, to include as wide a range of genes for phylogenetic analysis as possible.

For example, the most common gene to be used for constructing phylogenetic relationships in prokaryotes is the 16s rRNA gene since its sequences tend to be conserved among members with close phylogenetic distances, but variable enough that differences can be measured. However, in recent years it has also been argued that 16s rRNA genes can also be horizontally transferred. Although this may be infrequent, the validity of 16s rRNA-constructed phylogenetic trees must be reevaluated.[92]

Biologist Johann Peter Gogarten suggests ”the original metaphor of a tree no longer fits the data from recent genome research” therefore ”biologists should use the metaphor of a mosaic to describe the different histories combined in individual genomes and use the metaphor of a net to visualize the rich exchange and cooperative effects of HGT among microbes.”[31] There exist several methods to infer such phylogenetic networks.

Before it is transformed a bacterium is susceptible to antibiotics. A plasmid can be inserted when the bacteria is under stress, and be incorporated into the bacterial DNA creating antibiotic resistance. When the plasmids are prepared they are inserted into the bacterial cell by either making pores in the plasma membrane with temperature extremes and chemical treatments, or making it semi permeable through the process of electrophoresis, in which electric currents create the holes in the membrane. After conditions return to normal the holes in the membrane close and the plasmids are trapped inside the bacteria where they become part of the genetic material and their genes are expressed by the bacteria.

Gene transfer agent-release holin family

https://en.wikipedia.org/wiki/Gene_transfer_agent-release_holin_family

Selenocysteine (Sec) and pyrrolysine (Pyl) are rare amino acids that are cotranslationally inserted into proteins and known as the 21st and 22nd amino acids in the genetic code.

We identified 99 selenoprotein genes that clustered into 30 families, including 17 new selenoprotein genes that belong to six families.

How many water molecules can be detected by protein crystallography?

The number of water molecules which are expected to be experimentally located by protein crystallography was determined by multiple regression analysis on a test set of 873 known protein crystal structures.

https://www.ncbi.nlm.nih.gov/pubmed/10089359

Laminin

Laminins are high-molecular weight (~400 to ~900 kDa) proteins of the extracellular matrix. They are a major component of the basal lamina (one of the layers of the basement membrane), a protein network foundation for most cells and organs. The laminins are an important and biologically active part of the basal lamina, influencing cell differentiation, migration, and adhesion.

https://en.wikipedia.org/wiki/Laminin

Laminin is a protein that is part of the extracellular matrix in humans and animals. The extracellular matrix (ECM) lies outside of cells and provides support and attachment for cells inside organs (along with many other functions). Laminin has “arms” that associate with other laminin molecules to form sheets and bind to cells. Laminin and other ECM proteins essentially “glue” the cells (such as those lining the stomach and intestines) to a foundation of connective tissue. This keeps the cells in place and allows them to function properly. The structure of laminin is very important for its function (as is true for all proteins). One type of congenital muscular dystrophy results from defects in laminin.

An argument that has become quite common in modern Christianity is well illustrated by relation of the structure and function of laminin to biblical truths. This little, unknown protein became popular after it was used in a sermon. The topic of laminin quickly appeared in many emails and blogs, and eventually its shape made its way into merchandising (e.g., T-shirts and coffee mugs).

In a sermon, Louie Giglio asks how we can know that God will hold us together (which he infers from Psalm 33). He states, “That’s really what we want to know today, and I’ll tell you how you can know today that God will always hold you together, no matter what.”

Mr. Giglio then discusses the function of laminin (as glue), and its structure (a cross) in the body. He relates this to Colossians 1:17, which states, “He [Christ] is before all things, and in him all things hold together.” His argument is basically that God designed laminin in the shape of a cross and gave it the particular function of “glue” in the body so that we can know (in his words) the truth that Christ holds all things together.

Colossians 1:17 because it is God’s Word. Would Colossians 1:17 be any less true if laminin were not in the shape of a cross? No. If five years from now we discover that the laminin protein actually has a different shape (in fact, some electron micrographs of the protein do not resemble a cross at all, see here, p. 149), would that change the truth found in Colossians 1:17? No, because our belief in the truthfulness that Christ holds all things together should start and end with God’s Word alone!

 

Conclusion

Romans 1:20 makes it clear that we can know God through what He has made. God certainly designed the laminin protein and gave it a structure that allows it to perform the function He designated for it. In fact, one of the early papers on the structure and function of laminin said this: “Globular and rodlike domains are arranged in an extended four-armed, cruciform shape that is well suited for mediating between distant sites on cells and other components of the extracellular matrix” (emphasis mine).1

The supremacy of Christ that is talked about in Colossians 1:15–20 is probably one of my favorite passages in all of Scripture. Paul begins talking about Christ as Creator and moves to Christ as Redeemer. These are truths not because they appeal to our unaided reasoning, but because they are revealed in God’s Word.

https://answersingenesis.org/biology/microbiology/laminin-and-the-cross/

 

Colossians 1:15-17

 

The Supremacy of the Son of God

15 The Son is the image of the invisible God, the firstborn over all creation. 16 For in him all things were created: things in heaven and on earth, visible and invisible, whether thrones or powers or rulers or authorities; all things have been created through him and for him. 17 He is before all things, and in him all things hold together.

 

 

Genesis supermolecule – The Laminin protein or Laminin molecule – extracellular molecules – food and energy for the lightbody

 

 

Many are tjey looking for ”God particle” or ”God atom” per se – The Laminin molecule is God molcecule for the biomatrixgenesis of living creatures. GENESIS MEANING IS; Origin; production: biogenesis. GENES FROM ORIGINS.

Structure and function of laminin LG modules.

Laminin G domain-like (LG) modules of approximately 180-200 residues are found in a number of extracellular and receptor proteins and often are present in tandem arrays. LG modules are implicated in interactions with cellular receptors (integrins, alpha-dystroglycan), sulfated carbohydrates and other extracellular ligands. The recently determined crystal structures of LG modules of the laminin alpha2 chain reveal a compact beta sandwich fold and identify a novel calcium binding site. Binding epitopes for heparin, sulfatides and alpha-dystroglycan have been mapped by site-directed mutagenesis and show considerable overlap. The epitopes are located in surface loops around the calcium site, which in other proteins (agrin, neurexins) are modified by alternative splicing. Efficient ligand binding often requires LG modules to be present in tandem. The close proximity of the N- and C-termini in the LG module, as well as a unique link region between laminin LG3 and LG4, impose certain constraints on the arrangement of LG tandems. Further modifications may be introduced by proteolytic processing of laminin G domains, which is known to occur in the alpha2, alpha3 and alpha4 chains.

https://www.ncbi.nlm.nih.gov/pubmed/10963991

Extracellular matrix – Genesis supermolecule – The Laminin protein

In biology, the extracellular matrix (ECM) is a collection of extracellular molecules secreted by cells that provides structural and biochemical support to the surrounding cells.[1][2] Because multicellularity evolved independently in different multicellular lineages, the composition of ECM varies between multicellular structures; however, cell adhesion, cell-to-cell communication and differentiation are common functions of the ECM.

Role and importance

Due to its diverse nature and composition, the ECM can serve many functions, such as providing support, segregating tissues from one another, and regulating intercellular communication. The extracellular matrix regulates a cell’s dynamic behavior. In addition, it sequesters a wide range of cellular growth factors and acts as a local store for them.[4] Changes in physiological conditions can trigger protease activities that cause local release of such stores. This allows the rapid and local growth factor-mediated activation of cellular functions without de novo synthesis.

Molecular components

Components of the ECM are produced intracellularly by resident cells and secreted into the ECM via exocytosis.

Exocytosis

Exocytosis (/ˌɛkssˈtss/[1][2]) is a form of active transport in which a cell transports molecules (such as proteins) out of the cell (exo- + cytosis) by expelling them in an energy-using process. Exocytosis and its counterpart, endocytosis, are used by all cells because most chemical substances important to them are large polar molecules that cannot pass through the hydrophobic portion of the cell membrane by passive means.

In exocytosis, membrane-bound secretory vesicles are carried to the cell membrane, and their contents (water-soluble molecules such as proteins) are secreted into the extracellular environment. This secretion is possible because the vesicle transiently fuses with the outer cell membrane.

Exocytosis is also a mechanism by which cells are able to insert membrane proteins (such as ion channels and cell surface receptors), lipids, and other components into the cell membrane. Vesicles containing these membrane components fully fuse with and become part of the outer cell membrane.

https://en.wikipedia.org/wiki/Extracellular_matrix

Protein moonlighting

proteinmoon1

This article is about genes sharing multiple functions in an organism. For ”gene sharing” between organisms, see horizontal gene transfer.

Crystallographic structure of cytochrome P450 from the bacteria S. coelicolor (rainbow colored cartoon, N-terminus = blue, C-terminus = red) complexed with heme cofactor (magenta spheres) and two molecules of its endogenous substrate epi-isozizaene as orange and cyan spheres respectively. The orange-colored substrate resides in the monooxygenase site while the cyan-colored substrate occupies the substrate entrance site. An unoccupied moonlighting terpene synthase site is designated by the orange arrow.[1]

Protein moonlighting (or gene sharing) is a phenomenon by which a protein can perform more than one function.[2] Ancestral moonlighting proteins originally possessed a single function but through evolution, acquired additional functions. Many proteins that moonlight are enzymes; others are receptors, ion channels or chaperones. The most common primary function of moonlighting proteins is enzymatic catalysis, but these enzymes have acquired secondary non-enzymatic roles. Some examples of functions of moonlighting proteins secondary to catalysis include signal transduction, transcriptional regulation, apoptosis, motility, and structural.[3]

Protein moonlighting may occur widely in nature. Protein moonlighting through gene sharing differs from the use of a single gene to generate different proteins by alternative RNA splicing, DNA rearrangement, or post-translational processing. It is also different from multifunctionality of the protein, in which the protein has multiple domains, each serving a different function. Protein moonlighting by gene sharing means that a gene may acquire and maintain a second function without gene duplication and without loss of the primary function. Such genes are under two or more entirely different selective constraints.[4]

Various techniques have been used to reveal moonlighting functions in proteins. The detection of a protein in unexpected locations within cells, cell types, or tissues may suggest that a protein has a moonlighting function. Furthermore, sequence or structure homology of a protein may be used to infer both primary function as well as secondary moonlighting functions of a protein.

The most well-studied examples of gene sharing are crystallins. These proteins, when expressed at low levels in many tissues function as enzymes, but when expressed at high levels in eye tissue, become densely packed and thus form lenses. While the recognition of gene sharing is relatively recent—the term was coined in 1988, after crystallins in chickens and ducks were found to be identical to separately identified enzymes—recent studies have found many examples throughout the living world. Joram Piatigorsky has suggested that many or all proteins exhibit gene sharing to some extent, and that gene sharing is a key aspect of molecular evolution.[5]:1–7 The genes encoding crystallins must maintain sequences for catalytic function and transparency maintenance function.[4]

Inappropriate moonlighting is a contributing factor in some genetic diseases, and moonlighting provides a possible mechanism by which bacteria may become resistant to antibiotics.

Allosteric enzyme

Allosteric enzymes are enzymes that change their conformational ensemble upon binding of an effector, which results in an apparent change in binding affinity at a different ligand binding site. This ”action at a distance” through binding of one ligand affecting the binding of another at a distinctly different site, is the essence of the allosteric concept. Allostery plays a crucial role in many fundamental biological processes, including but not limited to cell signaling and the regulation of metabolism. Allosteric enzymes need not be oligomers as previously thought,[1] and in fact many systems have demonstrated allostery within single enzymes.[2] In biochemistry, allosteric regulation (or allosteric control) is the regulation of a protein by binding an effector molecule at a site other than the enzyme’s active site.

Allosteric regulations are a natural example of control loops, such as feedback from downstream products or feedforward from upstream substrates. Long-range allostery is especially important in cell signaling.[3] Allosteric regulation is also particularly important in the cell’s ability to adjust enzyme activity.

The term allostery comes from the Greek allos (ἄλλος), ”other,” and stereos (στερεὀς), ”solid (object).” This is in reference to the fact that the regulatory site of an allosteric protein is physically distinct from its active site.

The protein catalyst (enzyme) may be part of a multi-subunit complex, and/or may transiently or permanently associate with a Cofactor (e.g. adenosine triphosphate). Catalysis of biochemical reactions is vital due to the very low reaction rates of the uncatalysed reactions. A key driver of protein evolution is the optimization of such catalytic activities via protein dynamics.[4]

https://en.wikipedia.org/wiki/Allosteric_enzyme

Effector (biology)

In biochemistry, an effector molecule is usually a small molecule that selectively binds to a protein and regulates its biological activity. In this manner, effector molecules act as ligands that can increase or decrease enzyme activity, gene expression, or cell signalling. Effector molecules can also directly regulate the activity of some mRNA molecules (riboswitches).

https://en.wikipedia.org/wiki/Effector_(biology)

Cell signaling

Cell signaling (cell signalling in British English) is part of a complex system of communication that governs basic activities of cells and coordinates cell actions. The ability of cells to perceive and correctly respond to their microenvironment is the basis of development, tissue repair, and immunity as well as normal tissue homeostasis.

https://en.wikipedia.org/wiki/Cell_signaling

Conformational change

In biochemistry, a conformational change is a change in the shape of a macromolecule, often induced by environmental factors.

A macromolecule is usually flexible and dynamic. It can change its shape in response to changes in its environment or other factors; each possible shape is called a conformation, and a transition between them is called a conformational change.

https://en.wikipedia.org/wiki/Conformational_change

Macromolecule

A macromolecule is a very large molecule, such as protein, commonly created by polymerization of smaller subunits (monomers). They are typically composed of thousands of atoms or more. The most common macromolecues in biochemistry are biopolymers (nucleic acids, proteins, carbohydrates and polyphenols) and large non-polymeric molecules (such as lipids and macrocycles).[1] Synthetic macromolecules include common plastics and synthetic fibres as well as experimental materials such as carbon nanotubes.

DNA is optimised for encoding information

DNA is an information storage macromolecule that encodes the complete set of instructions (the genome) that are required to assemble, maintain, and reproduce every living organism.

DNA and RNA are both capable of encoding genetic information, because there are biochemical mechanisms which read the information coded within a DNA or RNA sequence and use it to generate a specified protein. On the other hand, the sequence information of a protein molecule is not used by cells to functionally encode genetic information.

https://en.wikipedia.org/wiki/Macromolecule

Proteins are optimised for catalysis

Proteins are functional macromolecules responsible for catalysing the biochemical reactions that sustain life.[1]:3 Proteins carry out all functions of an organism, for example photosynthesis, neural function, vision, and movement.

RNA is multifunctional

RNA is multifunctional, its primary function is to encode proteins, according to the instructions within a cell’s DNA.[1]:5 They control and regulate many aspects of protein synthesis in eukaryotes.

RNA encodes genetic information that can be translated into the amino acid sequence of proteins, as evidenced by the messenger RNA molecules present within every cell, and the RNA genomes of a large number of viruses. The single-stranded nature of RNA, together with tendency for rapid breakdown and a lack of repair systems means that RNA is not so well suited for the long-term storage of genetic information as is DNA.

https://en.wikipedia.org/wiki/Macromolecule

Complex systems

Complex systems present problems both in mathematical modelling and philosophical foundations. The study of complex systems represents a new approach to science that investigates how relationships between parts give rise to the collective behaviors of a system and how the system interacts and forms relationships with its environment

https://en.wikipedia.org/wiki/Complex_systems

The Holy Bible about Quantum Science – atoms and molecules

 The Four Electronic Quantum Numbers – Quantum Of light

”What about Ezekiel´s wheel recorded in the bible`? The description of what Ezekiel saw is clearly a link between heaven and earth. The description of the wheels seen by Ezekiel apperas to be a trans-dimensional portal. DNA is Gods language, and the language is Aleph-Tav, which forms the DNA helical wheel on the earth. There is an inner wheel with dreadfully high rims. This sounds like the DNA nucleotides bases. The outer wheel abobe the earth is described as four living creatures having four faces. Hyaluronic acid (HA) has four faces. All the information from chapter 1-10 of Ezekiel, demostrate that spirit of the living creature is in the wheels. Whithersoever the spirit was to go, they went, thither was their spirit to go; and the wheels were lifted up over against them; for the spirit of the living crature was in the wheels – Ezekiel 1:2”

Book of Revelation 4:6-9

Also in front of the throne there was what looked like a sea of glass, clear as crystal. In the center, around the throne, were four living creatures, and they were covered with eyes, in front and in back.
7 The first living creature was like a lion, the second was like an ox, the third had a face like a man, the fourth was like a flying eagle.
8 Each of the four living creatures had six wings and was covered with eyes all around, even under its wings. Day and night they never stop saying: “ ‘Holy, holy, holy is the Lord God Almighty,’who was, and is, and is to come.”
9 Whenever the living creatures give glory, honor and thanks to him who sits on the throne and who lives for ever and ever.

1. The DNA Strand is our Genetic code of life and Gods language

2. Laminin molecules holds allthing together

3. Helicase and the Hyaluronic acid (HA) has four faces (description of the crystal-like atom)

This molecules include DNA, Laminin and Hyaluronic acid (Helicase is the energy/fire and four wheels)

 

genesis-supermoleculeBildresultat för helicase molecule

DNA – HELICASE

G4-DNA – Quadruplexes – 4 strand DNA

 

Ezekiel Chapter 1 THE  4 WHEEL IS UNIVERSE MAGNETIC FIELD AND CIRCELS SPINNING AND MOVING LIKE SPINNING WHEELS, LIKE A WHIRLWIND

1 Now it came to pass in the thirtieth year, in the fourth month, in the fifth day of the month, as I was among the captives by the river of Chebar, that the heavens were opened, and I saw visions of God.

2 In the fifth day of the month, which was the fifth year of king Jehoiachin’s captivity,

3 The word of the LORD came expressly unto Ezekiel the priest, the son of Buzi, in the land of the Chaldeans by the river Chebar; and the hand of the LORD was there upon him.

4 And I looked, and, behold, a whirlwind came out of the north, a great cloud, and a fire infolding itself, and a brightness was about it, and out of the midst thereof as the colour of amber, out of the midst of the fire.

5 Also out of the midst thereof came the likeness of four living creatures. And this was their appearance; they had the likeness of a man.

6 And every one had four faces, and every one had four wings.

7 And their feet were straight feet; and the sole of their feet was like the sole of a calf’s foot: and they sparkled like the colour of burnished brass.

8 And they had the hands of a man under their wings on their four sides; and they four had their faces and their wings.

9 Their wings were joined one to another; they turned not when they went; they went every one straight forward.

10 As for the likeness of their faces, they four had the face of a man, and the face of a lion, on the right side: and they four had the face of an ox on the left side; they four also had the face of an eagle.

11 Thus were their faces: and their wings were stretched upward; two wings of every one were joined one to another, and two covered their bodies.

12 And they went every one straight forward: whither the spirit was to go, they went; and they turned not when they went.

13 As for the likeness of the living creatures, their appearance was like burning coals of fire, and like the appearance of lamps: it went up and down among the living creatures; and the fire was bright, and out of the fire went forth lightning.

14 And the living creatures ran and returned as the appearance of a flash of lightning.

15 Now as I beheld the living creatures, behold one wheel upon the earth by the living creatures, with his four faces.

16 The appearance of the wheels and their work was like unto the colour of a beryl: and they four had one likeness: and their appearance and their work was as it were a wheel in the middle of a wheel.

17 When they went, they went upon their four sides: and they turned not when they went.

18 As for their rings, they were so high that they were dreadful; and their rings were full of eyes round about them four.

19 And when the living creatures went, the wheels went by them: and when the living creatures were lifted up from the earth, the wheels were lifted up.

20 Whithersoever the spirit was to go, they went, thither was their spirit to go; and the wheels were lifted up over against them: for the spirit of the living creature was in the wheels.

21 When those went, these went; and when those stood, these stood; and when those were lifted up from the earth, the wheels were lifted up over against them: for the spirit of the living creature was in the wheels.

22 And the likeness of the firmament upon the heads of the living creature was as the colour of the terrible crystal, stretched forth over their heads above.

23 And under the firmament were their wings straight, the one toward the other: every one had two, which covered on this side, and every one had two, which covered on that side, their bodies.

24 And when they went, I heard the noise of their wings, like the noise of great waters, as the voice of the Almighty, the voice of speech, as the noise of an host: when they stood, they let down their wings.

25 And there was a voice from the firmament that was over their heads, when they stood, and had let down their wings.

26 And above the firmament that was over their heads was the likeness of a throne, as the appearance of a sapphire stone: and upon the likeness of the throne was the likeness as the appearance of a man above upon it.

27 And I saw as the colour of amber, as the appearance of fire round about within it, from the appearance of his loins even upward, and from the appearance of his loins even downward, I saw as it were the appearance of fire, and it had brightness round about.

28 As the appearance of the bow that is in the cloud in the day of rain, so was the appearance of the brightness round about. This was the appearance of the likeness of the glory of the LORD. And when I saw it, I fell upon my face, and I heard a voice of one that spake.

 Here is same quote back igen – what does this really mean in a nex context?

1 ”You have taken away the key to knowledge”? What knowledge…?
2. ”You yourselves have not entered”? Entered to what?
3. ”And you have hindered those who were entering” – Hindered to entering what?

This post is about life, evolving, knowledge, DNA, Genes, Genesis and the answer on these three questions is knowledge from the creator because the science have taken away the DNA code and key how to unzip your DNA code and the try to stop everyone frpm find it and hinde´red those who will and were entering. This qouate is about opening the 2 DNA strand west science tried to hide for decades.

expertsBildresultat för dna helicase

Bildresultat för dna helicaseBildresultat för dna helicase

2 DNA STRAND IS THE EVOLUTION CALLED

PSYCHICAL ( LIKE A PRISON, CLOSE UNIVERSE OR MAYBE HELL) AND LIMITATION OF LIFE AND A CLOSED UNIVERSE. IS 2 DNA STRAND SCIENCE DEMORACY OR JUST AWAY TO CONROL HUMAN AND THEIR EVOLUTION POSSIBILITIES AND ENLIGHTMENT

THIS IS HOW THEY UNSLAVE PEOPLE AND DON´T LIKE ENLIGHTMENT, WITHOUT KNOWLEDGE YOU ARE NOT FREE.

WEST WORLD SCIENCE LEARNING HUMANS BELIVE IN 2 DNA STRAND AND CALL THIS HUMANITY; FREEDOM AND DEMOCRACY; AND THOSE IN EAST WHO LEARNING AND BUILT SCIENCE ON BELIFE ON 12 DNA STRAND ARE COMMUNIST OR NO-DEMOCRACY. WHAT IS DEMOCRACY? 2 DNA ARE CLOSED SOCITIES, SECRET SOCITIES AND ELITE, FAKE GLOBEWORLD, EVOLUTIONS THEORY, DISTANCE TO SUN AND MOON; TIDES, THIS IS DEMOCRACY…CORRUPT MEDIA, MK-ULTRA MIND CONTROL, SURVEILLANCE….ALL THIS IS DEFINIED AS FREEDOM, AND HIDDEN SHADOW GOVERNMENT IS ALSO DEMOCRACY…CHEMITRAILS IS ASLO DEMOCRACY, WEATHER MANIPULATION, EARTHQUAKES, STORMS AND FLOODS IS MADE THIS SO CALLED HUMAN RACE, REAL IMAGES OF EARTH IS PHOTOSHOP AS THE MOST OTHER THINGS; EVEN THIS IS DEMOCRACY

HUMANS NEED TO OPEN OR UNZIP THE DOUBLE HELIX TO GET THE ENCLOSED INFORMATION IN THE OWN GENES.

THE TRUTH WILL SET YOU FREE (JESUS) AND UNZIP AND OPEN THE 12 DNA DOUBLE HELIX STRAND (THIS IS ABOUT MOLECULAR AND LIGHT OF FREEDOM). YOUR BODY IS BUILT UP ON ENERGY AND EVERYTHING IN LIFE; EARTH AND UNIVERS IS ENERGY.

Answers to quote Luke 11:52 is about our DNA going from 2 strand to 12 strand DNA, a upgading of your own DNA to a real world image. Who in the Bible could have interested from hiding this knowledge from humans to enslave humanity and control them?

  1. Our genetic information is safely locked up inside the double helix of DNA. In order to use this information, the helix must be unwound to expose the bases, allowing polymerases access to build complementary DNA or RNA strands. Unwinding of DNA is trickier than you might expect. The interaction between bases is quite strong and there are many, many of them, so it takes appreciable energy to separate the strands. This is the job of DNA helicases: they are enzymes that pull apart the two strands in a DNA double helix.
  2. The products of the ”reaction” then are single strands of DNA that have been unzipped and can then be replicated by other enzymes. Humans can developed new protein enzymes when the 2 DNA strand have been unzipped ”The genesis of the DNA-unwinding machinery is wonderfully complex and surprising,” How Helicase Unwinds the DNA Double Helix in Preparation for Replication
  3. DNA helicase pries apart the two strands in a DNA double helix, powered by ATP. Besides double helices and the above-mentioned triplexes, RNA and DNA can both also form quadruple helices. There are diverse structures of RNA base quadruplexes. Four consecutive guanine residues can form a quadruplex in RNA by Hoogsteen hydrogen bonds to form a “Hoogsteen ring”

Do you still belive 97-98% of your DNA are junk DNA?

prana10

Alchmical process – elightment – energy tranformation from materia to light (photons). This Bible qoute is about our inner light(body). Everything in life is energy.

Bildresultat för matt 19:30

The Alchemical process – where the smallest particle of light also becomes the largest because it connects with other light source – ”the least shall be the greatest” when the lightbody more and more become one with the light – and one with the consciousness and cosmic energy. Photons is more than just photons… molecular evolution…..in the state of being born – monatomic new bindning

Trees and timeline of the Bible

Timeline and the number of years people are said to have lived. Where genes better and more resilient than today? Can extracelluar molecules and foods from heaven and ”hidden manna” affect the lives. Diagram shows example on longevity

 

See bigger image link below

http://adam.bibelfokus.se/bild2.html

Extracellular molecules

Infogad bild 1

Infogad bild 2

 

Infogad bild 3

Infogad bild 4

Infogad bild 5

RNA polymerase

RNA polymerase (or, more fully, ribonucleic acid polymerase, abbreviated RNAP or RNApol), also known as DNA-dependent RNA polymerase, is an enzyme that produces primary transcript RNA. In cells,

Sigma factor

A sigma factor (σ factor) is a protein needed only for initiation of RNA synthesis.[1] It is a bacterial transcription initiation factor that enables specific binding of RNA polymerase to gene promoters. The specific sigma factor used to initiate transcription of a given gene will vary, depending on the gene and on the environmental signals needed to initiate transcription of that gene. Selection of promoters by RNA polymerase is dependent on the sigma factor that associates with it.

https://en.wikipedia.org/wiki/Sigma_factor

Promoter (genetics)

In genetics, a promoter is a region of DNA that initiates transcription of a particular gene. Promoters are located near the transcription start sites of genes, on the same strand and upstream on the DNA (towards the 5′ region of the sense strand). Promoters can be about 100–1000 base pairs long.

https://en.wikipedia.org/wiki/Promoter_(genetics)

RNA polymerase II

RNA polymerase II (RNAP II and Pol II) is an enzyme found in eukaryotic cells. It catalyzes the transcription of DNA to synthesize precursors of mRNA and most snRNA and microRNA.[2][3] A 550 kDa complex of 12 subunits, RNAP II is the most studied type of RNA polymerase. A wide range of transcription factors are required for it to bind to upstream gene promoters and begin transcription.

https://en.wikipedia.org/wiki/RNA_polymerase_II

In eukaryotes

The process is more complicated, and at least seven different factors are necessary for the binding of an RNA polymerase II to the promoter.

https://en.wikipedia.org/wiki/Promoter_(genetics)

Eukaryotic promoters are diverse and can be difficult to characterize, however, recent studies show that they are divided in more than 10 classes

Gene promoters are typically located upstream of the gene and can have regulatory elements several kilobases away from the transcriptional start site (enhancers). In eukaryotes, the transcriptional complex can cause the DNA to bend back on itself, which allows for placement of regulatory sequences far from the actual site of transcription. Eukaryotic RNA-polymerase-II-dependent promoters can contain a TATA element (consensus sequence TATAAA), which is recognized by the general transcription factor TATA-binding protein (TBP); and a B recognition element (BRE), which is recognized by the general transcription factor TFIIB.[3][7][8] The TATA element and BRE typically are located close to the transcriptional start site (typically within 30 to 40 base pairs).

Bidirectional (mammalian)

Bidirectional promoters are short (<1 kbp) intergenic regions of DNA between the 5′ ends of the genes in a bidirectional gene pair.[11] A “bidirectional gene pair” refers to two adjacent genes coded on opposite strands, with their 5′ ends oriented toward one another.[12] The two genes are often functionally related, and modification of their shared promoter region allows them to be co-regulated and thus co-expressed.[13] Bidirectional promoters are a common feature of mammalian genomes.[14] About 11% of human genes are bidirectionally paired.

https://en.wikipedia.org/wiki/Promoter_(genetics)

TATA-binding protein

The TATA-binding protein (TBP) is a general transcription factor that binds specifically to a DNA sequence called the TATA box. This DNA sequence is found about 30 base pairs upstream of the transcription start site in some eukaryotic gene promoters.[3] TBP, along with a variety of TBP-associated factors, make up the TFIID, a general transcription factor that in turn makes up part of the RNA polymerase II preinitiation complex.[4] As one of the few proteins in the preinitiation complex that binds DNA in a sequence-specific manner, it helps position RNA polymerase II over the transcription start site of the gene. However, it is estimated that only 10–20% of human promoters have TATA boxes. Therefore, TBP is probably not the only protein involved in positioning RNA polymerase II.

TBP is involved in DNA melting (double strand separation) by bending the DNA by 80° (the AT-rich sequence to which it binds facilitates easy melting). The TBP is an unusual protein in that it binds the minor groove using a β sheet.

Role as transcription factor

TBP is a subunit of the eukaryotic transcription factor TFIID. TFIID is the first protein to bind to DNA during the formation of the pre-initiation transcription complex of RNA polymerase II (RNA Pol II). Binding of TFIID to the TATA box in the promoter region of the gene initiates the recruitment of other factors required for RNA Pol II to begin transcription. Some of the other recruited transcription factors include TFIIA, TFIIB, and TFIIF. Each of these transcription factors is formed from the interaction of many protein subunits, indicating that transcription is a heavily regulated process.

TBP is also a component of RNA polymerase I and RNA polymerase III and is therefore involved in transcription initiation by all three RNA polymerases.[6] In specific cell types or on specific promoters TBP can be replaced by one of several TBP-related factors.[7]

https://en.wikipedia.org/wiki/TATA-binding_protein

RNA polymerase III

In eukaryote cells, RNA polymerase III (also called Pol III) transcribes DNA to synthesize ribosomal 5S rRNA, tRNA and other small RNAs.

The genes transcribed by RNA Pol III fall in the category of ”housekeeping” genes whose expression is required in all cell types and most environmental conditions. Therefore, the regulation of Pol III transcription is primarily tied to the regulation of cell growth and the cell cycle, thus requiring fewer regulatory proteins than RNA polymerase II. Under stress conditions however, the protein Maf1 represses Pol III activity.[

https://en.wikipedia.org/wiki/RNA_polymerase_III

Protein tertiary structure

Protein tertiary structure is the three dimensional shape of a protein. The tertiary structure will have a single polypeptide chain ”backbone” with one or more protein secondary structures, the protein domains. Amino acid side chains may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure.[1][2] A number of tertiary structures may fold into a quaternary structure.

Protein Tertiary Structure Retrieval Project (CoMOGrad)

Matching patterns in tertiary structure of a given protein to huge number of known protein tertiary structures and retrieve most similar ones in ranked order is in the heart of many research areas like function prediction of novel proteins, study of evolution, disease diagnosis, drug discovery, antibody design etc. The CoMOGrad project at BUET is a research effort to device an extremely fast and much precise method for protein tertiary structure retrieval and develop online tool based on research outcome. The developed online tool is available at http://research.buet.ac.bd:8080/Comograd/ . The pattern matching method is available at http://www.nature.com/articles/srep13275

https://en.wikipedia.org/wiki/Protein_tertiary_structure

Biopolymer

Biopolymers are polymers produced by living organisms; in other words, they are polymeric biomolecules. Since they are polymers, biopolymers contain monomeric units that are covalently bonded to form larger structures. There are three main classes of biopolymers, classified according to the monomeric units used and the structure of the biopolymer formed: polynucleotides (RNA and DNA), which are long polymers composed of 13 or more nucleotide monomers; polypeptides, which are short polymers of amino acids; and polysaccharides, which are often linear bonded polymeric carbohydrate structures.

The convention for a polypeptide is to list its constituent amino acid residues as they occur from the amino terminus to the carboxylic acid terminus. The amino acid residues are always joined by peptide bonds. Protein, though used colloquially to refer to any polypeptide, refers to larger or fully functional forms and can consist of several polypeptide chains as well as single chains. Proteins can also be modified to include non-peptide components, such as saccharide chains and lipids.

Nucleic acids

The convention for a nucleic acid sequence is to list the nucleotides as they occur from the 5′ end to the 3′ end of the polymer chain, where 5′ and 3′ refer to the numbering of carbons around the ribose ring which participate in forming the phosphate diester linkages of the chain. Such a sequence is called the primary structure of the biopolymer.

replication1

https://en.wikipedia.org/wiki/Biopolymer

Transcription factor II D

Coordinates the activities of more than 70 polypeptides required for initiation of transcription by RNA polymerase II

Transcription factor II D (TFIID) is one of several general transcription factors that make up the RNA polymerase II preinitiation complex. RNA polymerase II holoenzyme is a form of eukaryotic RNA polymerase II that is recruited to the promoters of protein-coding genes in living cells. It consists of RNA polymerase II, a subset of general transcription factors, and regulatory proteins known as SRB proteins. Before the start of transcription, the transcription Factor II D (TFIID) complex binds to the TATA box in the core promoter of the gene.

https://en.wikipedia.org/wiki/Transcription_factor_II_D

RNA polymerase II holoenzyme

RNA polymerase II holoenzyme is a form of eukaryotic RNA polymerase II that is recruited to the promoters of protein-coding genes in living cells.[1][2] It consists of RNA polymerase II, a subset of general transcription factors, and regulatory proteins known as SRB proteins.

https://en.wikipedia.org/wiki/RNA_polymerase_II_holoenzyme

Preinitiation complex

The preinitiation complex (PIC) is a large complex of proteins that is necessary for the transcription of protein-coding genes in eukaryotes and archaea. The PIC helps position RNA polymerase II over gene transcription start sites, denatures the DNA, and positions the DNA in the RNA polymerase II active site for transcription.[5]

The typical PIC is made up of six general transcription factors: TFIIA (GTF2A1, GTF2A2), TFIIB (GTF2B), B-TFIID (BTAF1, TBP), TFIID (BTAF1, BTF3, BTF3L4, EDF1, TAF1-15, 16 total), TFIIE, TFIIF, TFIIH and TFIIJ.

The construction of the polymerase complex takes place on the gene promoter. The TATA box is one well-studied example of a promoter element that occurs in approximately 10% of genes. It is conserved in many (though not all) model eukaryotes and is found in a fraction of the promoters in these organisms. The sequence TATA (or variations) is located at approximately 25 nucleotides upstream of the Transcription Start Point (TSP). In addition, there are also some weakly conserved features including the TFIIB-Recognition Element (BRE), approximately 5 nucleotides upstream (BREu) and 5 nucleotides downstream (BREd) of the TATA box.

https://en.wikipedia.org/wiki/RNA_polymerase_II_holoenzyme

TATA box

In molecular biology, the TATA box (also called the Goldberg-Hogness box)[2] is a DNA sequence (cis-regulatory element) found in the promoter region of genes in archaea and eukaryotes;[3] approximately 24% of human genes contain a TATA box within the core promoter.[4]

Considered to be the core promoter sequence, it is the binding site of either general transcription factors or histones (the binding of a transcription factor blocks the binding of a histone and vice versa) and is involved in the process of transcription by RNA polymerase.

The TATA box has the core DNA sequence 5′-TATAAA-3′ or a variant, which is usually followed by three or more adenine bases[citation needed]. It is usually located 25-35 base pairs upstream of the transcription start site. The sequence is believed to have remained consistent throughout much of the evolutionary process, possibly originating in an ancient eukaryotic organism.[6][7]

During the process of transcription, the TATA binding protein (TBP) normally binds to the TATA-box sequence, which unwinds the DNA and bends it through 80°. The AT-rich sequence of the TATA-box facilitates easy unwinding, due to weaker base-pairing interactions between A and T bases, as compared to between G and C. The TBP is an unusual protein in that it binds to the minor groove and binds with a β sheet.[8]

The TATA box is usually found at the binding site of RNA polymerase II. TFIID, a transcription factor, binds to the TATA box, followed by TFIIA binding to the upstream part of the TFIID protein. TFIIB then binds to the downstream part of TFIID.

RNA polymerase can then recognize this multi-protein complex and bind to it, along with various other transcription factors such as TFIIF, TFIIE and TFIIH. Transcription is then initiated, and the polymerase moves along the DNA strand, leaving TFIID and TFIIA bound to the TATA box. These can then facilitate the binding of additional RNA polymerase II molecules.

Most genes lack a TATA box and use an initiator element or downstream core promoter instead.[9] Nevertheless, TBP is always involved and is forced to bind without sequence specificity. A genome-wide study put the fraction of TATA-dependent human promoters at ~10%.[10] An earlier study of ~1,000 genes found 32% of the promoters had a TATA box.

https://en.wikipedia.org/wiki/TATA_box

MAF1

Repressor of RNA polymerase III transcription MAF1 homolog is a protein that in humans is encoded by the MAF1 gene.[3][4][5]

This gene encodes a protein that is homologous to Maf1, a Saccharomyces cerevisiae protein which is highly conserved in eukaryotic cells. S. cerevisiae Maf1 is a negative effector of RNA polymerase III (Pol III). It responds to changes in the cellular environment and represses Pol III transcription. Biochemical studies identified the initiation factor TFIIIB as a target for Maf1-dependent repression.

https://en.wikipedia.org/wiki/MAF1

50S

50S is the larger subunit of the 70S ribosome of prokaryotes. It is the site of inhibition for antibiotics such as macrolides, chloramphenicol, clindamycin, and the pleuromutilins. It includes the 5S ribosomal RNA and 23S ribosomal RNA.

50S, roughly equivalent to the 60S ribosomal subunit in eukaryotic cells, is the larger subunit of the 70S ribosome of prokaryotes. The 50S subunit is primarily composed of proteins but also contains single-stranded RNA known as ribosomal RNA (rRNA). rRNA forms secondary and tertiary structures to maintain the structure and carry out the catalytic functions of the ribosome.

X-ray crystallography has yielded electron density maps allowing the structure of the 50S in Haloarcula marismortui to be determined to 2.4Å resolution[1]and of the 50S in Deinococcus radiodurans to 3.3Å

Ribosomal RNA

The secondary structure of 23S is divided into six large domains, within which domain V is most important in its peptidyl transferase activity. Each domain contains normal secondary structure (e.g., base triple, tetraloop, cross-strand purine stack) and is also highly symmetric in tertiary structure; proteins intervene between their helices. At tertiary structure level, the large subunit rRNA is a single gigantic domain while the small subunit contains three structural domains. This difference reflects the lesser flexibility of the large subunit required by its function.

In chemistry, hydrophobicity is the physical property of a molecule (known as a hydrophobe) that is seemingly repelled from a mass of water.[1] (Strictly speaking, there is no repulsive force involved; it is an absence of attraction.) In contrast, hydrophiles are attracted to water.

Hydrophobic molecules tend to be nonpolar and, thus, prefer other neutral molecules and nonpolar solvents. Because water molecules are polar, hydrophobes do not dissolve well among them. Hydrophobic molecules in water often cluster together, forming micelles. Water on hydrophobic surfaces will exhibit a high contact angle.

The hydrophobic interaction is mostly an entropic effect originating from the disruption of the highly dynamic hydrogen bonds between molecules of liquid water by the nonpolar solute forming a clathrate-like structure around the non-polar molecules. This structure formed is more highly ordered than free water molecules due to the water molecules arranging themselves to interact as much as possible with themselves, and thus results in a higher entropic state which causes non-polar molecules to clump together to reduce the surface area exposed to water and decrease the entropy of the system.

Volvox and Microscopic scale

The microscopic scale (from Greek: μικρός, mikrós, ”small” and σκοπέω, skopéō ”look”) is the scale of objects and events smaller than those that can easily be seen by the naked eye, requiring a lens or microscope to see them clearly.[1] In physics, the microscopic scale is sometimes considered the scale between the macroscopic and the quantum regime.

By convention, the microscopic scale also includes classes of objects that are most commonly too small to see but of which some members are large enough to be observed with the eye. Such groups include the Cladocera, planktonic green algae of which Volvox is readily observable, and the protozoa of which stentor can be easily seen without aid. The submicroscopic scale similarly includes objects that are too small to see even with any optical microscope.

Volvox

Volvox is a polyphyletic genus of chlorophyte green algae in the family Volvocaceae. It forms spherical colonies of up to 50,000 cells. They live in a variety of freshwater habitats, and were first reported by Antonie van Leeuwenhoek in 1700. Volvox diverged from unicellular ancestors approximately 200 million years ago.

Volvox colony: 1) Chlamydomonas-like cell, 2) Daughter colony, 3) Cytoplasmic bridges, 4) Intercellular gel, 5) Reproductive cell, 6) Somatic cell.

Mikrofoto.de-volvox-4.jpg

Volvox is a genus of multicellular green algae.The cells have anterior eyespots that enable the colony to swim towards light. The cells of colonies in the more basal Euvolvox clade are interconnected by thin strands of cytoplasm, called protoplasmates.[4] Cell number is specified during development and is dependent on the number of rounds of division.

The cells of colonies in the more basal Euvolvox clade are interconnected by thin strands of cytoplasm, called protoplasmates.

https://en.wikipedia.org/wiki/Volvox

Cytoplasm

As a glass

Recently it has been proposed that the cytoplasm behaves like a glass-forming liquid approaching the glass transition.

The glass–liquid transition or glass transition for short is the reversible transition in amorphous materials (or in amorphous regions within semicrystalline materials) from a hard and relatively brittle ”glassy” state into a viscous or rubbery state as the temperature is increased.[1] An amorphous solid that exhibits a glass transition is called a glass. The reverse transition, achieved by supercooling a viscous liquid into the glass state, is called vitrification.

Crystallinity

Crystallinity refers to the degree of structural order in a solid. In a crystal, the atoms or molecules are arranged in a regular, periodic manner.

X-ray crystallography

Haloarcula

Haloarcula species are extreme halophilic archaea. They are distinguished from other genera in the Halobacteriaceae family by the presence of specific derivatives of TGD-2 polar lipids.

https://en.wikipedia.org/wiki/Haloarcula

Tertiary Structure

The overall three-dimensional shape of an entire protein molecule is the tertiary structure. The protein molecule will bend and twist in such a way as to achieve maximum stability or lowest energy state. Although the three-dimensional shape of a protein may seem irregular and random, it is fashioned by many stabilizing forces due to bonding interactions between the side-chain groups of the amino acids.

http://www.particlesciences.com/news/technical-briefs/2009/protein-structure.html

Last universal common ancestor

The last universal common ancestor (LUCA), also called the last universal ancestor (LUA), cenancestor, or progenote, is the most recent organism from which all organisms now living on Earth have a common descent.[1] LUCA is the most recent common ancestor of all current life on Earth. LUCA should not be assumed to be the first living organism on Earth. The LUCA is estimated to have lived some 3.5 to 3.8 billion years ago (sometime in the Paleoarchean era).[2][3] The composition of the LUCA is not directly accessible as a fossil, but can be studied by comparing the genomes of its descendents, organisms living today. By this means, a 2016 study identified a set of 355 genes inferred to have been present in the LUCA.[4]

The earliest evidence for life on Earth is biogenic graphite found in 3.7 billion-year-old metamorphized sedimentary rocks discovered in Western Greenland[5] and microbial mat fossils found in 3.48 billion-year-old sandstone discovered in Western Australia.[6][7] A 2015 study found potentially biogenic carbon from 4.1 billion years ago in ancient rocks in Western Australia, but such findings would indicate the existence of different conditions on Earth during that period than are generally assumed today, and point to an earlier origin of life.[8][9]

Charles Darwin proposed the theory of universal common descent through an evolutionary process in his book On the Origin of Species in 1859, saying, ”Therefore I should infer from analogy that probably all the organic beings which have ever lived on this earth have descended from some one primordial form, into which life was first breathed.

By analysis of the presumed LUCA’s offspring groups, the LUCA appears to have been a small, single-celled organism. It likely had a ring-shaped coil of DNA floating freely within the cell, like modern bacteria. Morphologically, it would likely not have been exceptionally distinctive among a collection of generalized, small-size, modern-day bacteria. However, Carl Woese et al, who first proposed the currently-used three domain system based on an analysis of rRNA sequences of bacteria, archaea, and eukaryotes, stated that the LUCA would have been a ”…simpler, more rudimentary entity than the individual ancestors that spawned the three [domains] (and their descendants)” regarding its genetic machinery.

The genetic code was most likely based on DNA.[16] Some studies suggest that the LUCA may have lacked DNA and been defined wholly through RNA.[17] If DNA was present, it was composed of four nucleotides (deoxyadenosine, deoxycytidine, deoxythymidine, and deoxyguanosine), to the exclusion of other possible deoxynucleotides. The DNA was kept double-stranded by a template-dependent enzyme, DNA polymerase. The integrity of the DNA was maintained by a group of maintenance enzymes, including DNA topoisomerase, DNA ligase and other DNA repair enzymes. The DNA was also protected by DNA-binding proteins such as histones. The genetic code was composed of three-nucleotide codons, thus producing 64 different codons. Since only 20 amino acids were used, multiple codons code for the same amino acids.[12][13][14][15] If the code was DNA-based, it operated as follows. The genetic code was expressed via RNA intermediates, which were single-stranded. The RNA was produced by a DNA-dependent RNA polymerase using nucleotides similar to those of DNA, with the exception that the nucleotide thymidine in DNA was replaced by uridine in RNA.[12][13][14][15]

The genetic code was expressed into proteins. These were assembled from free amino acids by translation of a messenger RNA by a mechanism composed of ribosomes, transfer RNAs, and a group of related proteins. The ribosomes were composed of two subunits, one big 50S and one small 30S. Each ribosomal subunit was composed of a core of ribosomal RNA surrounded by ribosomal proteins. Both types of RNA molecules (ribosomal and transfer RNAs) played an important role in the catalytic activity of the ribosomes. Only 20 amino acids were used, to the exclusion of countless other amino acids. Only the L-isomers of the amino acids were used. ATP was used as an energy intermediate. Several hundred enzymes made of protein catalyzed chemical reactions that extract energy from fats, sugars, and amino acids, and that synthesize fats, sugars, amino acids, and nucleic acid bases using arbitrary chemical pathways.

https://en.wikipedia.org/wiki/Last_universal_common_ancestor

Three Of Life and DNA strand

Bildresultat för tree of life and DNA STRAND

RecA

RecA is a 38 kilodalton protein essential for the repair and maintenance of DNA.[2] A RecA structural and functional homolog has been found in every species in which one has been seriously sought and serves as an archetype for this class of homologous DNA repair proteins. The homologous protein is called RAD51 in eukaryotes and RadA in archaea.

RecA has multiple activities, all related to DNA repair. In the bacterial SOS response, it has a co-protease [3] function in the autocatalytic cleavage of the LexA repressor and the λ repressor.[4]

RecA’s association with DNA major is based on its central role in homologous recombination. The RecA protein binds strongly and in long clusters to ssDNA to form a nucleoprotein filament. The protein has more than one DNA binding site, and thus can hold a single strand and double strand together. This feature makes it possible to catalyze a DNA synapsis reaction between a DNA double helix and a complementary region of single stranded DNA

RAD51

RAD51 is a eukaryote gene. The protein encoded by this gene is a member of the RAD51 protein family which assists in repair of DNA double strand breaks. RAD51 family members are homologous to the bacterial RecA, Archaeal RadA and yeast Rad51.[3] The protein is highly conserved in most eukaryotes, from yeast to humans.

n mammals, seven recA-like genes have been identified: Rad51, Rad51L1/B, Rad51L2/C, Rad51L3/D, XRCC2, XRCC3, and DMC1/Lim15.[5] All of these proteins, with the exception of meiosis-specific DMC1, are essential for development in mammals. Rad51 is a member of the RecA-like NTPases.

In humans, RAD51 is a 339-amino acid protein that plays a major role in homologous recombination of DNA during double strand break repair. In this process, an ATP dependent DNA strand exchange takes place in which a template strand invades base-paired strands of homologous DNA molecules. RAD51 is involved in the search for homology and strand pairing stages of the process.

Unlike other proteins involved in DNA metabolism, the RecA/Rad51 family forms a helical nucleoprotein filament on DNA.

https://en.wikipedia.org/wiki/RAD51

Homologous recombination

Homologous recombination is a type of genetic recombination in which nucleotide sequences are exchanged between two similar or identical molecules of DNA. It is most widely used by cells to accurately repair harmful breaks that occur on both strands of DNA, known as double-strand breaks. Homologous recombination also produces new combinations of DNA sequences during meiosis.

Homologous recombination is conserved across all three domains of life as well as viruses, suggesting that it is a nearly universal biological mechanism.

Although homologous recombination varies widely among different organisms and cell types, most forms involve the same basic steps. After a double-strand break occurs, sections of DNA around the 5′ ends of the break are cut away in a process called resection. In the strand invasion step that follows, an overhanging 3′ end of the broken DNA molecule then ”invades” a similar or identical DNA molecule that is not broken. After strand invasion, the further sequence of events may follow either of two main pathway.

Heterotrimeric G protein

”G protein” usually refers to the membrane-associated heterotrimeric G proteins, sometimes referred to as the ”large” G proteins (as opposed to the subclass of smaller, monomeric small GTPases) . These proteins are activated by G protein-coupled receptors and are made up of alpha (α), beta (β) and gamma (γ) subunits,[1] the latter two referred to as the beta-gamma complex.

https://en.wikipedia.org/wiki/Heterotrimeric_G_protein

G beta-gamma complex

The G beta-gamma complex (Gβγ) is a tightly bound dimeric protein complex, composed of one Gβ and one Gγ subunit, and is a component of heterotrimeric G proteins. Heterotrimeric G proteins, also called guanosine nucleotide-binding proteins, consist of three subunits, called alpha, beta, and gamma subunits, or Gα, Gβ, and Gγ. When a G protein-coupled receptor (GPCR) is activated, Gα dissociates from Gβγ, allowing both subunits to perform their respective downstream signaling effects. One of the major functions of Gβγ is the inhibition of the Gα subunit.

This heterotrimeric G protein is illustrated with its theoretical lipid anchors. GDP is black. Alpha chain is yellow. Beta-gamma complex is blue. Membrane is Grey.

Laminin protein – the human protein Atlas

Laminins are high-molecular weight (~400 to ~900 kDa) proteins of the extracellular matrix. They are a major component of the basal lamina (one of the layers of the basement membrane), a protein network foundation for most cells and organs. The laminins are an important and biologically active part of the basal lamina, influencing cell differentiation, migration, and adhesion.

Laminin is the name used for a family of proteins that serve many useful functions in biology. The most important property of laminins is their ability to easily bind to each other and to other proteins. This makes laminin a critical means of holding tissues and organs together. It has been described as the protein equivalent of glue, though it functions differently than actual chemical glue will.

 

Laminins are large heterotrimeric glycoproteins.

Laminins are heterotrimeric proteins that contain an α-chain, a β-chain, and a γ-chain, found in five, four, and three genetic variants, respectively.

Laminins, composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively), have a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric.

Relaterad bild

Human proteins containing laminin domains

Laminin Domain I

LAMA1; LAMA2; LAMA3; LAMA4; LAMA5;

Laminin Domain II

LAMA1; LAMA2; LAMA3; LAMA4; LAMA5;

Laminin B (Domain IV)

HSPG2; LAMA1; LAMA2; LAMA3; LAMA5; LAMC1; LAMC2; LAMC3;

Laminin EGF-like (Domains III and V)

AGRIN; ATRN; ATRNL1; CELSR1; CELSR2; CELSR3; CRELD1; HSPG2; LAMA1; LAMA2; LAMA3; LAMA4; LAMA5; LAMB1; LAMB2; LAMB3; LAMB4; LAMC1; LAMC2; LAMC3; MEGF10; MEGF12; MEGF6; MEGF8; MEGF9; NSR1; NTN1; NTN2L; NTN4; NTNG1; NTNG2; RESDA1; SCARF1; SCARF2; SREC; STAB1; USH2A;

Laminin G domain

AGRIN; CELSR1; CELSR2; CELSR3; CNTNAP1; CNTNAP2; CNTNAP3; CNTNAP3B; CNTNAP4; CNTNAP5; COL11A1; COL11A2; COL12A1; COL14A1; COL15A1; COL16A1; COL18A1; COL19A1; COL20A1; COL21A1; COL22A1; COL24A1; COL27A1; COL5A1; COL5A3; COL9A1; CRB1; CRB2; CSPG4; EGFLAM; EYS; FAT; FAT2; FAT3; FAT4; GAS6; HSPG2; LAMA1; LAMA2; LAMA3; LAMA4; LAMA5; NELL1; NELL2; NRXN1; NRXN2; NRXN3; PROS1; SLIT1; SLIT2; SLIT3; SPEAR; THBS1; THBS2; THBS3; THBS4; USH2A;

Laminin N-terminal (Domain VI)

LAMA1; LAMA2; LAMA3; LAMA5; LAMB1; LAMB2; LAMB3; LAMB4; LAMC1; LAMC3; NTN1; NTN2L; NTN4; NTNG1; NTNG2; USH2A;

https://en.wikipedia.org/wiki/Laminin

Glycoprotein

Glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to polypeptide side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated.

https://en.wikipedia.org/wiki/Glycoprotein

Laminin subunit alpha 3 – LAMA3 gene

The LAMA3 gene provides instructions for making one part (subunit) of a protein called laminin 332 (formerly known as laminin 5). This protein is made up of three subunits, called alpha, beta, and gamma. The LAMA3 gene carries instructions for the alpha subunit; the beta and gamma subunits are produced from other genes. Three versions of the alpha subunit, called alpha-3a, alpha-3b1, and alpha-3b2, are produced from the LAMA3 gene. The protein encoded by this gene is the alpha-3 chain of laminin 5, which is a complex glycoprotein composed of three subunits (alpha, beta, and gamma).

Laminin subunit gamma-1 is a protein that in humans is encoded by the LAMC1 gene.

 

https://en.wikipedia.org/wiki/Laminin,_alpha_3

Laminins are a group of proteins that regulate cell growth, cell movement (motility), and the attachment of cells to one another (adhesion). They are also involved in the formation and organization of basement membranes, which are thin, sheet-like structures that separate and support cells in many tissues. Laminin 332 has a particularly important role in the basement membrane that underlies the top layer of skin (the epidermis). This membrane gives strength and resiliency to the skin and creates an additional barrier between the body and its surrounding environment. Laminin 332 is a major component of fibers called anchoring filaments, which connect the two layers of the basement membrane and help hold the skin together.

Studies suggest that laminin 332 also has several other functions. This protein appears to be important in the formation of early wound-healing tissues.

The alpha subunit produced from the LAMA3 gene is also part of two other laminin proteins, laminin 311 and laminin 321. These laminins also appear to provide strength to the skin, although they do not play as big a role as laminin 332. In addition, laminin 311 is involved in cell signaling in the lungs and other tissues.

https://ghr.nlm.nih.gov/gene/LAMA3

 

Laminin – Role in neural development

Laminin-111 is a major substrate along which nerve axons will grow, both in vivo and in vitro. For example, it lays down a path that developing retinal ganglion cells follow on their way from the retina to the tectum. It is also often used as a substrate in cell culture experiments. Interestingly, the presence of laminin-1 can influence how the growth cone responds to other cues. For example, growth cones are repelled by netrin when grown on laminin-111, but are attracted to netrin when grown on fibronecti. This effect of laminin-111 probably occurs through a lowering of intracellular cyclic AMP

The netrins are a family of laminin-related molecules.

The netrins are a family of laminin-related molecules. Here, we characterize a new member of the family, beta-netrin. beta-Netrin is homologous to the NH(2) terminus of laminin chain short arms; it contains a laminin-like domain VI and 3.5 laminin EGF repeats and a netrin C domain. Unlike other netrins, this new netrin is more related to the laminin beta chains, thus, its name beta-netrin. An initial analysis of the tissue distribution revealed that kidney, heart, ovary, retina, and the olfactory bulb were tissues of high expression. We have expressed the molecule in a eukaryotic cell expression system and made antibodies to the expressed product. Both in situ hybridization and

Cartoon of laminin and netrin families. Three classes of netrin molecules have been described; netrins 1–3 are more related to laminin γ chains, whereas the netrin reported here, β-netrin, is more related to the laminin β chains. Two additional molecules, one of which is a putative transmembrane molecule and are homologous to the short arm of laminin chains, have been found (see text for details; for simplicity they are shown along side the α chain). Thus, there is a growing family of molecules which have homology to the short arms of laminin molecules.Bildresultat för laminin molecule

 

This gene encodes the gamma chain isoform laminin, gamma 2. The gamma 2 chain, formerly thought to be a truncated version of beta chain (B2t), is highly homologous to the gamma 1 chain; however, it lacks domain VI, and domains V, IV and III are shorter. It is expressed in several fetal tissues but differently from gamma 1, and is specifically localized to epithelial cells in skin, lung and kidney. The gamma 2 chain together with alpha 3 and beta 3 chains constitute laminin 5 (earlier known as kalinin),

multidomain protein encoded by a distinct gene The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the gamma chain isoform laminin, gamma 1. The gamma 1 chain, formerly thought to be a beta chain, contains structural domains similar to beta chains, however, lacks the short alpha region separating domains I and II. The structural organization of this gene also suggested that it had diverged considerably from the beta chain genes.

 

 

https://openi.nlm.nih.gov/detailedresult.php?img=PMC2192657_JCB0007020.f11&req=4

The trimeric proteins intersect to form a cross-like structure that can bind to other cell membrane and extracellular matrix molecules.[4] The three shorter arms are particularly good at binding to other laminin molecules, which allows them to form sheets. The long arm is capable of binding to cells, which helps anchor organized tissue cells to the membrane.

The laminin family of glycoproteins are an integral part of the structural scaffolding in almost every tissue of an organism. They are secreted and incorporated into cell-associated extracellular matrices. Laminin is vital for the maintenance and survival of tissues.

 

 

ADAM (protein)

In humans, there are 19 Adam genes

Proposed scenario for the evolutionary history of ADAMTS proteins. During chordate evolution a series of gene duplications resulted in six ADAMTS proteins present in the Ciona genome, while an early retrotransposition event gave rise to the ”angiogenesis clade” of ADAMTS proteins. This proliferation of ADAMTS proteins did not occur in invertebrates, and there is evidence of the loss of one ADAMTS ortholog from Caenorhabditis. More recent duplications that occurred early during  vertebrate evolution resulted in the paired sets of ADAMTS proteins present in the human genome.

The chromosomal locations of the human ADAMTS genes are indicated in parentheses and the exon structure of each human gene is diagrammed to the right of its position in the schematic phylogenetic tree,

Proposed scenario for the evolutionary history of ADAMTS proteins. During chordate evolution a series of gene duplications resulted in six ADAMTS proteins present in the Ciona genome, while an early retrotransposition event gave rise to the "angiogenesis clade" of ADAMTS proteins. This proliferation of ADAMTS proteins did not occur in invertebrates, and there is evidence of the loss of one ADAMTS ortholog from Caenorhabditis. More recent duplications that occurred early during vertebrate evolution resulted in the paired sets of ADAMTS proteins present in the human genome. The chromosomal locations of the human ADAMTS genes are indicated in parentheses and the exon structure of each human gene is diagrammed to the right of its position in the schematic phylogenetic tree, and shown in more detail in the Additional Files.

A second evolutionarily related group is comprised of ADAMTS1, -4, -5, -8 and -15 and their single sister in Ciona. Vertebrate members of this group share unique intron positions and lack all of the intron positions held by other ADAMTS genes and their invertebrate homologs (Figure 3). Three members of this group (ADAMTS1, -4, and -8) encode proteins with aggrecanase and angiogenesis-related functions, which suggests the examination of ADAMTS5 and -15 for similar biological activities. This putative ”angiogenesis/aggrecanase group” appears most closely related to ADAMTS20 and -9. Further, the unique intron positions shared by ADAMTS1, -4, -5, -8, and -15, and lack of invertebrate orthologs in this putative ”angiogenesis/aggrecanase group” suggest that this group’s progenitor arose within chordates via a retrotransposition event from the common ancestor of the group comprised by ADAMTS20 and -9 (Figures 2 and 4). The intron/exon structures of ADAMTS1, -4, -5, -8, and -15 are similar to that of the mouse ADAMTS1 gene [63], and our analysis shows four ADAMTS genes with this characteristic gene structure in the genome of F. rubripes. Therefore, retrotransposition of an ancestor of the angiogenesis/aggrecanase subfamily of genes, its acquisition of new introns, and subsequent gene duplications that produced five related genes occurred prior to the divergence of human, mouse and pufferfish lineages. In at least one case (intron 17 in ADAMTS8) we see evidence of acquisition of a new intron following the process of duplication, but prior to the divergence of mammals and pufferfish.

https://www.researchgate.net/figure/8038709_fig4_Proposed-scenario-for-the-evolutionary-history-of-ADAMTS-proteins-During-chordate

The 19 human ADAMTS proteins can be assembled into eight ‘clades’ on the basis of their domain organization and their known functions. The aggrecanase and proteoglycanase clades (ADAMTS1, 4, 5, 8, 15, and ADAMTS9 and 20) can cleave hyaluronan-binding chondroitin sulfate proteoglycan (CSPG) extracellular proteins, including aggrecan, versican, brevican and neurocan [5]. This sub-group has also been labeled ‘angioinhibitory’ on the basis of the original identification of ADAMTS1 and 8 as anti-angiogenic factors [6]; nevertheless, ADAMTSs in other clades also have effects on angiogenesis. Another group (ADAMTS2, 3 and 14) are pro-collagen N-propeptidases that are essential for the maturation of triple helical collagen fibrils. 

Bildresultat för triple helical collagen fibrilsRelaterad bild

Collagen’s triple helical structure, known as the Madras helix, was first proposed by G. N. Ramachandran and G. Kartha in 1954. The collagen molecule subunit (tropocollagen) is a rod made up of three left-handed helices (distinct from the right handed alpha helix). The three helices are twisted together into a right-handed coiled coil. Collagen is distinguished by the regular arrangement of amino acids in each of the three chains of these collagen subunits. Glycine nearly always occurs at every third residue, proline makes up about 9% of collagen and hydroxylproline (Hyp) and hydroxylysine are also found. These latter two are both the uncommon results of post translational modifications. The sequence normally follows the pattern Gly-Pro-Y or Gly-X-Hyp, where X and Y may be any of various other amino acid residues. Gly-Pro-Hyp occurs particularly frequently and this regular repetition and high glycine content is found in only a few other fibrous proteins, including silk fibroin (another fibre of high tensile strength). Each chain is over 1400 amino acids long.

Righthanded (clockwise) or left-handed (anti-clockwise)

Handbook of Proteolytic Enzymes

Handbook of Proteolytic Enzymes – ADAMS PROTEINS

ACTG2

Actin, gamma-enteric smooth muscle is a protein that in humans is encoded by the ACTG2gene.[3][4][5]

Actins are highly conserved proteins that are involved in various types of cell motility, and maintenance of the cytoskeleton. In vertebrates, three main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton, and as mediators of internal cell motility. Actin, gamma 2, encoded by this gene, is a smooth muscle actin found in enteric tissues.

https://en.wikipedia.org/wiki/ACTG2

Emerin

Emerin is a protein that in humans is encoded by the EMD gene, also known as the STA gene. Emerin, together with MAN1, is a LEM domain-containing integralprotein of the innernuclear membrane in vertebrates. Emerin is highly expressed in cardiac and skeletal muscle. In cardiac muscle, emerin localizes to adherens junctions within intercalated discs where it appears to function in mechanotransduction of cellular strain and in beta-catenin signaling.

Emerin is a serine-rich nuclear membrane protein and a member of the nuclear lamina-associated protein family.

https://en.wikipedia.org/wiki/Emerin

Nuclear lamina

DNA replication

Various experiments show that the nuclear lamina plays a part in the elongation phase of DNA replication. It has been suggested that lamins provide a scaffold, essential for the assembly of the elongation complexes, or that it provides an initiation point for the assembly of this nuclear scaffold.

Not only nuclear lamina associated lamins are present during replication, but free lamin polypeptides are present as well and seem to have some regulative part in the replication process.

Elongation

DNA polymerase has 5′-3′ activity. All known DNA replication systems require a free 3′ hydroxyl group before synthesis can be initiated (note: the DNA template is read in 3′ to 5′ direction whereas a new strand is synthesized in the 5′ to 3′ direction—this is often confused). Four distinct mechanisms for DNA synthesis are recognized

https://en.wikipedia.org/wiki/DNA_replication#Elongation

DNA repair

Repair of DNA double-strand breaks can occur by either of two processes, non-homologous end joining (NHEJ) or homologous recombination (HR). A-type lamins promote genetic stability by maintaining levels of proteins that have key roles in NHEJ and HR.[3] Mouse cells deficient for maturation of prelamin A show increased DNA damage and chromosome aberrations and are more sensitive to DNA damaging agents.

https://en.wikipedia.org/wiki/Nuclear_lamina

DNA Helicase

History of DNA helicases

DNA helicases were discovered in E. coli in 1976. This helicase was described as a ”DNA unwinding enzyme” that is ”found to denature DNA duplexes in an ATP-dependent reaction, without detectably degrading”.[11] The first eukaryotic DNA helicase was in 1978 in the lily plant.[12] Since then, DNA helicases were discovered and isolated in other bacteria, viruses, yeast, flies, and higher eukaryotes.[13] To date, at least 14 different helicases have been isolated from single celled organisms, 6 helicases from bacteriophages, 12 from viruses, 15 from yeast, 8 from plants, 11 from calf thymus, and approximately 25 helicases from human cells.[14] Below is a history of helicase discovery:

  • 1976 – Discovery and isolation of E. coli-based DNA helicase[11]
  • 1978 – Discovery of the first eukaryotic DNA helicases, isolated from the lily plant[12]
  • 1982 – ”T4 gene 41 protein” is the first reported bacteriophage DNA helicase[13]
  • 1985 – First mammalian DNA helicases isolated from calf thymus[15]
  • 1986 – SV40 large tumor antigen reported as a viral helicase (1st reported viral protein that was determined to serve as a DNA helicase)[16]
  • 1986 – ATPaseIII, a yeast protein, determined to be a DNA helicase[17]
  • 1988 – Discovery of seven conserved amino acid domains determined to be helicase motifs
  • 1989 – Designation of DNA helicase Superfamily I and Superfamily II[18]
  • 1989 – Identification of the DEAD box helicase family[19]
  • 1990 – Isolation of a human DNA helicase[20]
  • 1992 – Isolation of the first reported mitochondrial DNA helicase (from bovine brain)[21]
  • 1996 – Report of the discovery of the first purified chloroplast DNA helicase from the pea[22]
  • 2002 – Isolation and characterization of the first biochemically active malarial parasite DNA helicase – Plasmodium cynomolgi.[23]

https://en.wikipedia.org/wiki/Helicase

RecQ helicases: multiple structures for multiple functions

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2714954/

Mechanisms of a ring shaped helicase

Structural basis for DNA strand separation by a hexameric replicative helicase

4093251

Crystal Structure of T7 Gene 4 Ring Helicase Indicates a Mechanism for Sequential Hydrolysis of Nucleotides

The basic activity of a helicase is the separation of nucleic acid duplexes into their component strands, a process that is coupled to the hydrolysis of NTPs. However, there are 12 known DNA helicases in E. coli that perform a variety of tasks in nucleic acid metabolism, ranging from simple strand separation at the replication fork (e.g., DnaB helicase) to more elaborate processes such as the migration of Holliday junctions (e.g., RuvAB complex). Helicases can be divided into two classes on the basis of mechanism, those that translocate in a 5′–3′ direction along single-stranded DNA and those that operate with the opposite polarity. For the 3′–5′ helicases, there has been a considerable amount of recent structural and biochemical data to enlighten our understanding of the mechanism of these enzymes. The first crystal structure of a helicase was that of PcrA ( Subramanya et al. 1996). The structure revealed that the enzyme comprised several domains, including two domains that are structurally similar to the ATPase domain of the recombination protein RecA (Story and Steitz 1992), despite minimal sequence homology with one another or with RecA. The E. coli Rep helicase ( Korolev et al. 1997) and NS3 RNA helicase (Kim et al. 1998) were also crystallized with single-stranded DNA, giving the first glimpses of how the proteins interact with nucleic acids.

http://www.sciencedirect.com/science/article/pii/S0092867400808715

The Gene 4 Protein of Bacteriophage T7 CHARACTERIZATION OF HELICASE ACTIVITY

www.jbc.org/content/258/22/14017.full.pdf

Bacteriophage T7 gene 2.5 protein: An essential protein for DNA replication

http://www.pnas.org/content/90/21/10173.full.pdf

Independence helicase and T7 4 Gene proteein (Google books)

Energy Coupling and Molecular Motors – Google Books

https://en.wikipedia.org/wiki/G_beta-gamma_complex

https://en.wikipedia.org/wiki/Microscopic_scale

https://en.wikipedia.org/wiki/Molecular_evolution

https://en.wikipedia.org/wiki/Protein_dynamics

https://en.wikipedia.org/wiki/Amino_acid

https://en.wikipedia.org/wiki/Enzyme

https://en.wikipedia.org/wiki/Allosteric_regulation

https://en.wikipedia.org/wiki/Morpheein

https://en.wikipedia.org/wiki/Genetic_code

https://en.wikipedia.org/wiki/Chemical_reaction

https://en.wikipedia.org/wiki/Aminoacyl_tRNA_synthetase

https://en.wikipedia.org/wiki/Adaptability

https://en.wikipedia.org/wiki/Ecological_resilience

https://en.wikipedia.org/wiki/Phenotype

https://en.wikipedia.org/wiki/Protomer

https://en.wikipedia.org/wiki/Generating_set_of_a_group

 

https://en.wikipedia.org/wiki/DNA_polymerase

 

https://en.wikipedia.org/wiki/Natural_selection

https://en.wikipedia.org/wiki/Chemical_reaction

https://en.wikipedia.org/wiki/Metabolic_pathway

https://en.wikipedia.org/wiki/DNA_polymerase

https://en.wikipedia.org/wiki/Mobile_genetic_elements