Studies of collagen fold formation in aqueous solutions of α-gelatin III

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 partic...

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Veröffentlicht in:	Biopolymers 1984-02, Vol.23 (2), p.353-361
Hauptverfasser:	Thorn, I., Eagland, D.
Format:	Artikel
Sprache:	eng
Schlagworte:	Biological and medical sciences Chemical Phenomena Chemistry, Physical Collagen Conformational dynamics in molecular biology Fundamental and applied biological sciences. Psychology Gelatin Molecular biophysics Protein Conformation Viscosity
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Zusammenfassung:	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.
ISSN:	0006-3525 1097-0282
DOI:	10.1002/bip.360230213