Protein hydration in aqueous solution.
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.
Otting
G
G
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.
Liepinsh
E
E
Wüthrich
K
K
D000818:Animals; D002417:Cattle; D003461:Crystallography; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010121:Oxytocin / Q000737:chemistry*; D010179:Pancreas / Q000201:enzymology; D011487:Protein Conformation; D012996:Solutions; D014361:Trypsin Inhibitors / Q000737:chemistry* / Q000648:ultrastructure; D014867:Water; D014961:X-Ray Diffraction
D012996:Solutions; D014361:Trypsin Inhibitors; D014867:Water; D010121:Oxytocin