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Studies of collagen fold formation in aqueous solutions of α‐gelatin III
Author(s) -
Thorn I.,
Eagland D.
Publication year - 1984
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.360230213
Subject(s) - chemistry , gelatin , reversion , aqueous solution , alcohol , solvent , optical rotation , viscosity , crystallography , polymer chemistry , biophysics , biochemistry , organic chemistry , thermodynamics , physics , biology , gene , phenotype
Optical rotation, viscosity, and density studies are reported on solutions of α‐gelatin in solvent mixtures of water and various monohydric alcohols. Reversion to the collagen fold by the protein is shown to be order in all cases, but changes in magnitude as a function of concentration of the particular alcohol are observed. The structuring effects of the alcohol on water are seen to be reflected in the extent of helix regeneration by the protein. Shorter chain alcohols appear to influence the initial rate of reversion by direct interaction with the protein.