Abstract:
Clathrate hydrates form the basis of a general model of biomolecule hydration. In clathrate hydrate crystal structures, the size of hydrogen-bonded water rings is highly constrained to five members. The clathrate hydrate model predicts that the size of water rings near biomolecule surfaces is similarly constrained to five members. This report describes a test of this model of biomolecule hydration. We have demonstrated that five-membered water rings are not a general feature of protein or nucleic acid hydration. The clathrate hydrate model appears to be inappropriate for soluble biomolecules. (C) 1996 John Wiley and Sons, Inc.

KeyWords Plus:
WATER-STRUCTURE, RESOLUTION, PROTEIN, CRYSTALS, CRAMBIN

Addresses:
GEORGIA INST TECHNOL, SCH CHEM and BIOCHEM, ATLANTA, GA 30332-0400.

Publisher:
JOHN WILEY and SONS INC, NEW YORK

IDS Number:
TR391

ISSN:
0006-3525