A collagen model peptide comprising three covalently cross-linked chains (Ala-Gly-ProIg with a stable triple-helix conformation was utilized as the constant part of elongated model peptides of different composition.
Influence of different tripeptides on the stability of the collagen triple helix. I. Analysis of the collagen sequence and identification of typical tripeptides
✍ Scribed by R. Dölz; E. Heidemann
- Book ID
- 102765978
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1986
- Tongue
- English
- Weight
- 545 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
The amino acid sequence of the collagen al(1) chain (cal0 is analyzed. Deviations of random tripeptide distribution leads to the definition of clusters. Inside these regions, collagen-typical tripeptides are located. Besides Gly-Pro-Hyp, Gly-PreAla, and Gly-Ala-Hyp, the polar sequences Gly-Glu-Hyp, Gly-Ala-Arg, Gly-Glu-Arg, and Gly-Pro-Lys form typical sequences. The neighborhood of each tripeptide is analyzed and classified. The proximity to the collagen-typical tripeptides is registered. Cluster theory: Less-typical sequences also fold as members of the collagen triple helix and they are as reasonable as well as important for the collagen structure as the cluster tripeptides, but only the latter are important for the nucleation of the triplehelical folding.
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