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Abstract
The acid-soluble collagen of calf-skin in aqueous medium was denatured by heating above a critical temperature T M. The helix- coil transition of collagen in water-organic solvents mixtures was measured by polarimetry. The water-methanol systems raise the T M, which is considerably decreased by water-amide, water-chlorinated alcohols or water dimethylsulphoxide mixtures. An attempt is made to correlate these results with the possible interactions between organic solvents and protein.
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