ISSN:
0006-3525
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
A collagen model peptide comprising three covalently cross-linked chains (Ala-Gly-Pro)8 with a stable triple-helix conformation was utilized as the constant part of elongated model peptides of different composition. The tripeptides Gly-Pro-Hyp, Gly-Pro-Ala, Gly-Pro-Pro, Gly-Pro-Ser, Gly-Ala-Hyp, Gly-Phe-Hyp, Gly-Glu-Hyp, Gly-Ala-Lys, and Gly-Pro-Phe were coupled at the N-terminal to the cross-linked peptide. The transition temperatures determined by CD measurements are higher for the peptides containing the Gly-X-Hyp sequences followed by those with the Gly-Pro-Y sequences. In experiments with combinations of two different tripeptides coupled to the constant part of the cross-linked model peptides higher transition temperatures were observed if the sequence of helix-promoting tripeptides was not interrupted.
Additional Material:
3 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bip.360250608
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