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Stabilization of collagen structure: Dependence of collagen denaturation enthalpy on the imino acid content
Author(s) -
Burjanadze T. V.
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.360210809
Subject(s) - chemistry , hydroxyproline , imino acid , enthalpy , denaturation (fissile materials) , proline , crystallography , thermodynamics , amino acid , nuclear chemistry , biochemistry , physics
An analysis of the available data on the enthalpy (Δ H r ) of denaturation (melting) of collagens with different imino acid content in solution and in the aggregated state has shown that Δ H r in solution increases with increasing denaturation temperature, whereas in the aggregated state there is an inverse dependence. Δ H r in solution correlates with the hydroxyproline content but not with that of proline. No correlation between the change of Δ H r and the imino acid content is observed for the aggregated state.