collagen

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Uses

  • when partially hydrolyzed, the three tropocollagen strands separate into globular, random coils, producing gelatin

Function

Structure

  • long, fibrous structural protein with triple helical structure, known as the Madras helix.
  • tropocollagen or collage subunit is a rod about 300 nm long & 1.5 nm in diameter, made up of three polypeptide strands, each of which is a left-handed helix#
  • the 3 left-handed helices are twisted together into a right-handed coiled-coil, stabilized by hydrogen bonds.
  • tropocollagen subunits spontaneously self-assemble, with regularly staggered ends, into even larger arrays in the extracellular matrix of tissue
  • some covalent crosslinking occurs within the triple helices
  • variable amount of covalent crosslinking between tropocollagen helices
  • tropocollagen from young animals can be extracted because it is not yet fully crosslinked
  • a distinctive feature of collagen is the regular arrangement of amino acid residues in each of the 3 chains of collagen
  • repeats of Gly-X-Pro or Gly-X-Hyp, where X may any amino acid residues
  • in collagen, Gly is required at every 3rd position because the assembly of the triple helix puts this residue at the interior (axis) of the helix, where there is no space for a larger side group
  • the rings of the Pro & Hyp must point outward
  • Pro & Hyp thermally stabilize the triple helix, Hyp more so than Pro
  • in bone, entire collagen triple helices lie in a parallel, staggered array
  • 40 nm gaps between the ends of the tropocollagen subunits probably serve as nucleation sites for the deposition of long, hard, fine crystals of the mineral component, hydroxyapatite
  • in this way that certain types of cartilage turn into bone
  • collagen fibrils are collagen molecules packed into an organized overlapping bundle
  • collagen fibers are bundles of fibrils.

# alpha helix is right-handed

Compartment

Expression

formation of collagen:

Pathology

Pharmacology

More general terms

More specific terms

Additional terms

References

  1. Wikipedia, collagen entry http://en.wikipedia.org/wiki/collagen
  2. Di Lullo GA et al Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen. J Biol Chem. 2002 Feb 8;277(6):4223-31. Epub 2001 Nov 9. PMID: https://www.ncbi.nlm.nih.gov/pubmed/11704682