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Bound water in the collagen‐like triple‐helical structure
Author(s) -
Lazarev Yuri A.,
Grishkovsky Boris A.,
Khromova Tatyana B.,
Lazareva Alisa A.,
Grechishko Vera S.
Publication year - 1992
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.360320209
Subject(s) - chemistry , hydrogen bond , triple helix , collagen helix , amide , hydrate , crystallography , triple bond , helix (gastropod) , bound water , peptide , peptide bond , stereochemistry , molecule , polymer chemistry , organic chemistry , double bond , biochemistry , ecology , snail , biology
The ir amide bands of the triple‐helical polytripeptides and collagens upon hydration of films are investigated. On the basis of our assignment of the amide I components, the formation of hydrogen bonds between the peptide backbone and structural water is studied. The C 1 O 1 —HOH hydrogen bonds are found more ordered than the C 3 O 3 —HOH hydrogen bonds. The specific incorporation of water in the triple helix is followed by multistep conformational changes and by increasing of the interpeptide hydrogen‐bond strength. The formation of the polypeptide hydrate structure depending on the amino acid composition and the chain length is examined.