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 | The image on the right-hand side has each side chain colored a different color to shown how each individual <scene name='Sandbox_168/Helices/1'>α-helices</scene> interact 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. | have also been illustrated to point out their positions in the triple-helix. | ||
