Solvation energy and thermal stability of hydrophilization-modified alpha-chymotrypsin.

Abstract

As reported in the literature [Mozhaev et al. (1988), Eur. J. Biochem. 173, 147-154], when a series of modifiers, especially the cyclic anhydrides of pyromellitic and mellitic acids, are introduced into each lysine located in the alpha-chymotrypsin (CT) surface, a substantial hydrophilization of the enzyme surface can occur and remarkable stabilization… (More)

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