Stabilization of collagen structure: Dependence of collagen denaturation enthalpy on the imino acid content | Zendy

Burjanadze T. V. | Zendy

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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.

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