Abstract
THE contribution of water to the stability of macromolecular structures of biological origin is often difficult to assess. Besides its intrinsic theoretical interest1,2, this problem is of great practical importance in studies concerned with the preparation of single crystals of proteins3 and nucleic acids from an aqueous mother liquor as well as in studies of such macromolecules in non-aqueous solvents4. For these reasons we believe that the detailed study of physicochemical changes which accompany the excessive dehydration of proteins and nucleic acids might be of considerable value. In this communication, we wish to report evidence that gelatine becomes covalently cross-linked when the water content falls below about 0.2 g/100 g protein.
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YANNAS, I., TOBOLSKY, A. Cross-linking of Gelatine by Dehydration. Nature 215, 509–510 (1967). https://doi.org/10.1038/215509b0
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DOI: https://doi.org/10.1038/215509b0
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