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Science 15 November 1991:
Vol. 254. no. 5034, pp. 974 - 980
DOI: 10.1126/science.1948083
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Articles

Science, Vol 254, Issue 5034, 974-980
Copyright © 1991 by American Association for the Advancement of Science

articles

Protein hydration in aqueous solution

G Otting, E Liepinsh, and K Wuthrich

Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische Hochschule-Honggerberg, Zurich, Switzerland.

High-resolution proton nuclear magnetic resonance studies of protein hydration in aqueous solution show that there are two qualitatively different types of hydration sites. A well-defined, small number of water molecules in the interior of the protein are in identical locations in the crystal structure and in solution, and their residence times are in the range from about 10(-2) to 10(-8) second. Hydration of the protein surface in solution is by water molecules with residence times in the subnanosecond range, even when they are located in hydration sites that contain well-ordered water in the x-ray structures of protein single crystals.


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