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Dependence of thermal stability on the number of hydrogen bonds in water‐bridged collagen structure
Author(s) -
Burjanadze T. V.,
Kisiriya E. L.
Publication year - 1982
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.360210902
Subject(s) - thermostability , chemistry , hydrogen bond , hydroxyproline , imino acid , thermal stability , polymer chemistry , crystallography , proline , organic chemistry , amino acid , enzyme , biochemistry , molecule
The probable number of hydrogen bonds has been calculated as a function of the imino acid content for water‐bridged collagen structures. With increasing imino acid content in collagen, the number of hydrogen bonds stabilizing triple‐helical structures become saturation. This might explain the asymptotic character of the empirical relation between thermostability and hydroxyproline content for collagen.