Otting G, Liepinsh E, Wüthrich K
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.
Science. 1991 Nov 15;254(5034):974-80. doi: 10.1126/science.1948083.
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.
对水溶液中蛋白质水合作用的高分辨率质子核磁共振研究表明，存在两种性质不同的水合位点。蛋白质内部有数量明确的少数水分子，它们在晶体结构和溶液中的位置相同，其停留时间在约10⁻²到10⁻⁸秒的范围内。即使位于蛋白质单晶X射线结构中含有有序水的水合位点，溶液中蛋白质表面的水合作用也是由停留时间在亚纳秒范围内的水分子进行的。
