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Topic: Collagen helix


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  Collagen
Collagen is the main protein of connective tissue.
Collagen also fills out the cornea[?] where it is present in crystalline form.
Type III collagen - This is the collagen of granulation tissue[?], and is produced quickly by young fibroblasts before the tougher type I collagen is synthesised.
www.ebroadcast.com.au /lookup/encyclopedia/co/Collagen.html   (218 words)

  
 Collagen
Collagen is a major component of the connective tissue meshwork that runs through animal bodies.
The helix forming region is composed predominantly of three amino acids: glycine, which occurs in every third position throughout the long sequence; proline, which frequently follows glycine in this segment, and alanine.
Glycine is the smallest of the amino acids and in the collagen triple helix, the glycines of adjacent polypeptide chains are packed close together.
www.algoart.com /music/collagen.htm   (476 words)

  
 Biochemist Solves Riddle Of Collagen Stability
Collagen breakdown is at the heart of many serious diseases, such as arthritis, rheumatism, brittle bones, lupus, cirrhosis and cataracts.
Collagen is created by cells with a complex and repeated chain of amino acids, with different helices performing specialized tasks in the body.
The stability of collagen is measured by its "melting point," or the temperature at which the strands begin to unravel, Raines said.
www.eurekalert.org /pub_releases/1998-04/UoW-BSRO-220498.php   (782 words)

  
 The Importance of Calorad's Collagen
Collagen is a family of highly characteristic fibrous proteins found in all multicellular animals which are the most abundant proteins found in mammals, constituting 25 percent of the total protein mass.
Type I is the principle collagen of skin and bone and, by far, the most abundant in the body (representing 90 per cent of body collagen).
As we age, function of the fibroblast family of cells to produce collagen compounds diminishes, which then reduces the gel-like substances of the extra-cellular matrix that protects cells and tissues from the compression of life and exercise.
www.collagenweightloss.com /collagen_report.php4   (2163 words)

  
 Collagen and Natural Gut Strings
The packing of collagen molecules is stabilized by covalent aldol cross-links between lysine or hydroxylysine residues at the C-terminus of one collagen molecule and the N-terminus of an adjacent one.
As collagen is strained beyond its yield point, the crosslinks between fibrils break and defibrillation and eventually failure occurs.
The mechanical properties of fibrous collagen networks with low levels of crosslinking between fibrils are dominated by the viscous sliding of collagen molecules and fibrils.
web.mit.edu /3.082/www/team1_f02/collagen.htm   (1131 words)

  
 Collagen Water Structure Revealed
Collagen is the main protein in connective tissues of animals and the most abundant protein in mammals.
The collagen molecule is a rod about 300 nm long and 1.5 nm in diameter, made up of three polypeptide subunits wrapped around one another in a triple helix.
Type I collagen has a mean molecular weight per amino acid residue of 91.2 Daltons (a Dalton is a unit of mass equivalent to 1 g), which is calculated from the amino acid sequences of the polypeptide chains.
www.i-sis.org.uk /Collagenwaterstructurerevealed.php   (1419 words)

  
 LifeSource LABS - Collagen
Collagen is the main component of our skin, nails, bones, cartilage, and connective tissue and is found in all of the body organs.
Collagen protein also includes red blood cells and albumin, which serves to regulate body processes as well as being an essential component of thousands of enzymes and hormones that also regulate the fluid and electrolyte balance in the body.
The LifeSource Concentrated Collagen™ is a liquid nutritional supplement with a delicious flavor that, thanks to our patented enzymatic process, offers the body raw material necessary to preserve the essential collagen in a natural form, which in turn will help with all areas of your body from head to toes.
lifesourcelabs.com /collagen.html   (4900 words)

  
 Pfam 21.0 : Collagen
Collagens are generally extracellular structural proteins involved in formation of connective tissue structure.
Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure.
Collagens are post-translationally modified by proline hydroxylase to form the hydroxyproline residues.
pfam.janelia.org /cgi-bin/getdesc?acc=PF01391   (213 words)

  
 extracellular matrix I
Collagen is the most abundant protein in the body, about 50% of body protein is collagen.
Collagens are largely synthesised by fibroblasts in most tissues, chondrocytes in cartilage, osteoblasts in bone, pericytes in blood vessels.
Excessive collagen degradation is observed in several diseases, e.g., degradation of cartilage collagen in rheumatoid arthritis and bone collagen in osteoporosis.
www.sgul.ac.uk /depts/histopathology/ECMI.html   (871 words)

  
 Fish Gelatin
Collagen is the major structural protein found in the skin and bones of all animals.
The collagen molecule consists of 3 individual polypeptide chains (alpha chains) which are wound around one another in a triple helix confirmation.
The fish collagen consisted primarily of alpha 1 and alpha 2 chains in a 2:1 ratio.
www.norlandprod.com /techrpts/fishgelrpt.html   (1905 words)

  
 PDB Molecule of the Month:Collagen   (Site not responding. Last check: 2007-08-11)
Collagen is a major structural protein, forming molecular cables that strengthen the tendons and vast, resilient sheets that support the skin and internal organs.
Collagen is composed of three chains, wound together in a tight triple helix.
Collagen from livestock animals is a familiar ingredient for cooking.
pdbdev.sdsc.edu:48346 /pdb/molecules/pdb4_1.html   (371 words)

  
 Kinked Collagen VI Tetramers and Reduced Microfibril Formation as a Result of Bethlem Myopathy and Introduced Triple ...
Collagen VI tetramers from all of the mutant
Collagen VI chains in the eluted fractions were detected on dot blots with the 3C4 antibody.
Two collagen VI monomers (gray and fl) are associated in an antiparallel fashion with a stagger of 30 nm and an overlap of 75 nm.
www.jbc.org /cgi/content/full/277/3/1949   (5687 words)

  
 Collagen & Bone: Collagen
Collagen is body’s major frame work protein, are rod shaped, fibrous proteins insoluble in water.
Collagen has triple helical structure leading to aggregation of collagen monomers into long fibres, which is an elongated structure unlike compact globular proteins.
A normal modification of collagen that accumulates during life is the oxidation of some lysine side chains, producing covalent cross-links between tropocollagen fibers.
w3.ouhsc.edu /dentalbiochemistry/madhu/COLLAGEN.htm   (816 words)

  
 Vitamin C and Collagen   (Site not responding. Last check: 2007-08-11)
The synthesis of collagen, for which vitamin C is essential, proceeds in the body as one of its major manufacturing enterprises.
Collagen is a protein, one of the thousands of different kinds of proteins in the human body.
Collagen as strong white fibers, stronger than steel wire of the same weight, and as yellow elastic networks (called elastin), usually together with macropolysaccharides, constitutes the connective tissue that holds our bodies together.
www.vitamincfoundation.org /collagen.html   (1063 words)

  
 Alpha helix - Wikipedia, the free encyclopedia
The amino acids in an α helix are arranged in a right-handed helical structure, 5.4 Å (= 0.54 nm) wide.
A helix has an overall dipole moment caused by the aggregate effect of all the individual dipoles from the carbonyl groups of the peptide bond pointing along the helix axis.
This is because of the convenient structural fact that the diameter of the α helix is 1.2 nanometres, the same as the width of the major groove in B-form DNA.
en.wikipedia.org /wiki/Alpha_helix   (1985 words)

  
 About Our Company - Collagen3H
Inflammation and collagen remodeling may lead to the loss of pigment-producing, melanocyte cells or obscuring of melanin pigment.
The invention of fish collagen that is biologically active, meaning that it has retained the Triple Helix structure making it identical to the human collagen, is the single greatest breakthrough in the field of cosmetics and dermatology in this and the last century.
Collagen and elastin are proteins that support the structure of cells in our bodies.
www.collagen3h.com /site/1009093/page/45030   (1621 words)

  
 Direct Science Chemistry - Collagen
Collagen, a triple helical structure, is a protein is a major component of the connective tissues.
Collagen consists of three left-handed polyproline II-like chains supercoiled in a parallel direction with one-residue shift, resulting in a right-handed superhelix.
This article "Collagen" is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 2.5 License and is copyrighted by Boyang Zhao.
www.directscience.info /chemistry/collagen   (306 words)

  
 Chemicon - Product #CC078 - Bovine Collagen Type III
Dissolved collagen retains the ability to form microfibrils, activate platelet aggregation and serve as a substrate for cell growth in culture.
Collagen is extracted from washed dissected tissue into dilute acetic acid after mild pepsin treatment.
Add Lyophilized collagen to 0.5 M acedic acid (3% glacial acetic acid v/v in water), 0.8 mg of solution to each mg of collagen.
www.chemicon.com /browse/productdetail.asp?ProductID=CC078   (209 words)

  
 Collagen   (Site not responding. Last check: 2007-08-11)
This is collagen, the fibrous structural protein that makes up skin, bones, tendons, blood vessels, and corneas.
In order to form the collagen helix, you need a repeating pattern of glycine, proline, and hydroxyproline in the backbone.
Collagen fibers are cross linked between another modified amino acid, hydroxylysine (not shown in this image).
faculty.gvsu.edu /carlsont/mm/proteins/collagen.htm   (103 words)

  
 Collagen mutations and genotype-phenotype correlation
The full phenotypic range of OI is caused by mutations in the two chains that comprise type I collagen, the major protein of the extracellular matrix of bone, skin and tendon.
The collagen genes are organized with each exon coding for the helical region beginning with a glycine codon and ending with codon for a Y position; therefore the skipping of a helical exon does not cause a frameshift in the collagen transcript.
In the α1(I) chain, the mutations may disrupt the stability of the collagen helix itself.
www.endotext.org /parathyroid/parathyroid17/ch01s03.html   (810 words)

  
 Collagen
Collagen is the most abundant protein in mammals.
The collagen fibres consist of globular units of the collagen sub-unit tropocollagen.
Another rare feature of collagen is its regular arrangement of amino acids in each of the alpha chains of the collagen sub-units.
www.3dchem.com /molecules.asp?ID=195   (459 words)

  
 The Ramachandran diagram.
X-Ray structure of the triple helical collagen model peptide (Pro-Hyp-Gly)10 in which the fifth Gly is replaced by Ala.
The H helix of sperm whale myoglobin: a skeletal model.
The H helix of sperm whale myoglobin: a space-filling model.
www.nd.edu /~aseriann/CHAP8B.html   (751 words)

  
 +Bones & Joints ++Save The Bones Save Our Lives
At the bottom, the helix is less regular, because many different amino acids are placed between the equally-spaced glycines.
We make many different kinds of collagen, which form long ropes and tough sheets that are used for structural support in mature animals and as pathways for cellular movement during development.
Type IV collagen has a globular head at one end and an extra tail at the other.
www.freewebs.com /bones_joints/collagenresearch.htm   (742 words)

  
 Chemicon - Product #CC076 - Human Collagen Type IV
Collagen type IV is the major structural element of basal membranes.
Human collagen type IV is a native triple helix.
The Collagen type IV was purified by using differential salt precipitation.
www.chemicon.com /browse/productdetail.asp?ProductID=CC076   (200 words)

  
 Biochemistry Faculty   (Site not responding. Last check: 2007-08-11)
The collagen triple-helix motif, with its (Gly-X-Y)n repeating sequence and high content of imino acids, is a major structural element in all collagens and also constitutes an important domain in the macrophage scavenger receptor, C1q, collectins and the asymmetric form of acetylcholinesterase.
The research goals of this laboratory, funded by NIH and the Children’s Brittle Bone Foundation, are to use biophysical studies on peptides models to clarify the basic features of the triple-helix and its structural abnormalities in diseased states.
Studies on peptides that model mutations found in type I collagen in Osteogenesis imperfecta, a disease characterized by fragile bones, to investigate the consequences of these mutations on stability, folding and dynamics.
www2.umdnj.edu /bchemweb/HTML/BrodskyNEW.html   (391 words)

  
 PIRSF Entry
Collagens are the primary structural proteins in the body and are usually found in connective tissues.
The collagen type VI monomer is composed of large globular domains at each end linked by triple helical repeats.
Collagen type VI consists of a vWA domain and collagen triple helix repeats.
pir.georgetown.edu /cgi-bin/ipcSF?id=PIRSF002259   (422 words)

  
 Type I Collagen Triplet Duplication Mutation in Lethal Osteogenesis Imperfecta Shifts Register of alpha Chains ...
helix folding in the manner of a glycine substitution.
Matrix was extracted serially, first with NaCl to isolate newly incorporated collagen without cross-links (matrix fraction 1) and then with acetic acid for immaturely cross-linked collagen (matrix fraction 2) and finally with pepsin to release fully cross-linked collagen (matrix fraction 3).
Propagation of the register shift for the entire length of the helix may affect the kinetics of N-propeptide cleavage (32-34).
www.jbc.org /cgi/content/full/278/12/10006   (4949 words)

  
 Problem Set II
Explain why mutations in the glycine residues of collagen are particularly devastating.
The small glycine residues are crucial for the formation of the triple helix of collagen, which is the basic building block of the collagen fiber.
Collagen monomers assemble into the triple-helical rod starting from their amino-terminal ends.
cmgm.stanford.edu /biochem200/PS2.htm   (751 words)

  
 Structural Aspects Osteogenesis imperfecta
Collagen is a fibrous protein that provides structural and functional integrity in the human body.
An understanding of the physical properties of native and mutant collagens will provide the basis for comprehending the etiology of OI phenotypes at the molecular level.
We are using molecular dynamics and free energy of denaturation calculations to compute the energetic and structural consequences of single point mutations and correlate the magnitude of these changes with the experimentally observed data with the phenotypic severity of OI.
www.cgl.ucsf.edu /Research/oi   (383 words)

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