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• W2005746614 abstract "The collagen triple-helix consists of a repeating (Gly-X-Y)n sequence. In theory, there are more than 400 possible Gly-X-Y triplets, but analysis of sequences from fibrillar and nonfibrillar collagens shows that only a limited set of triplets are found in significant numbers, and many are never observed. The nonrandom frequency of Gly-X-Y triplets makes it practical to experimentally approach the stability of much of the collagen sequence through the study of a limited set of host-guest peptides. In these peptides, individual Gly-X-Y triplets constitute the guest, while the host consists of Gly-Pro-Hyp tripeptides. A set of host-guest peptides was designed to contain the most common nonpolar and charged triplets found in collagen. All formed stable triple-helices, with their melting temperature depending on the identity of the guest triplet. While including less than 10% of all possible triplets, the data set covers 50-60% of collagen sequences and provides a starting point for establishing a stability scale to predict the relative stability of important collagen regions, such as the matrix metalloproteinase cleavage site or binding sites." @default.
• W2005746614 created "2016-06-24" @default.
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• W2005746614 date "1998-01-01" @default.
• W2005746614 modified "2023-10-14" @default.
• W2005746614 title "Gly-X-Y Tripeptide Frequencies in Collagen: A Context for Host–Guest Triple-Helical Peptides" @default.
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• W2005746614 doi "https://doi.org/10.1006/jsbi.1998.3977" @default.
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