Collagen Structure & Function: Difference between revisions
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These three chains are then twisted around one another in a rope-like manner to produce the overall tightly packed triple-helical form of the molecule. The interaction of α-chains is stabilized via interchain hydrogen bonding making the molecule fairly resistant to attack by other molcules. This hydrogen bonding occurs when the amino group (NH) of a glycine residue forms a peptide bond with the carbonyl (C=0) of an adjacent residue. The overall molecule is approxiametly 300nm long and 1.5-2nm in diameter <ref>PMID: 7695699 </ref>. | These three chains are then twisted around one another in a rope-like manner to produce the overall tightly packed triple-helical form of the molecule. The interaction of α-chains is stabilized via interchain hydrogen bonding making the molecule fairly resistant to attack by other molcules. This hydrogen bonding occurs when the amino group (NH) of a glycine residue forms a peptide bond with the carbonyl (C=0) of an adjacent residue. The overall molecule is approxiametly 300nm long and 1.5-2nm in diameter <ref>PMID: 7695699 </ref>. | ||
The image on the right-hand side has each side chain colored a different color to shown how each individual protein chain interacts with the others to form the overall molecule. The active sites have also been illustrated to point out their positions in the triple-helix. | The image on the right-hand side has each side chain colored a different color to shown how each individual protein chain interacts with the others to form the overall molecule. The <scene name='Sandbox_168/Myscene/1'>active sites</scene> | ||
have also been illustrated to point out their positions in the triple-helix. | |||
==Function== | ==Function== | ||
