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Influence of different tripeptides on the stability of the collagen triple helix. I. Analysis of the collagen sequence and identification of typical tripeptides
Author(s) -
Dölz R.,
Heidemann E.
Publication year - 1986
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360250607
Subject(s) - tripeptide , collagen helix , chemistry , triple helix , sequence (biology) , oligopeptide , stereochemistry , folding (dsp implementation) , crystallography , amino acid , helix (gastropod) , peptide , biochemistry , biology , ecology , snail , electrical engineering , engineering
The amino acid sequence of the collagen α1(I) chain (calf) 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‐Pro‐Ala, 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 triple‐helical folding.