DYNAMICAL DEDUCTIONS FROM NUCLEAR MAGNETIC-RESONANCE RELAXATION MEASUREMENTS AT THE WATER-PROTEIN INTERFACE
DYNAMICAL DEDUCTIONS FROM NUCLEAR MAGNETIC-RESONANCE RELAXATION MEASUREMENTS AT THE WATER-PROTEIN INTERFACE
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DOI：
10.1016/s0006-3495(80)84912-5
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发表时间：
1980-01-01
影响因子：
3.4
通讯作者：
SHIRLEY, WM
中科院分区：
文献类型：
--
作者：
BRYANT, RG;SHIRLEY, WM
核磁共振(核磁共振)测量提供了关于观察到核共振的分子的结构和动力学信息。这篇手稿介绍了蛋白质粉体系中水质子的核磁共振弛豫。包含了水质子自旋和蛋白质质子自旋之间的磁通讯，使得对蛋白质表面的水分子动力学的了解比以前更清晰。我们得出结论，水分子在蛋白质表面的运动比在无溶质溶剂中的运动要慢一些，但即使在水合到远低于通常认为的蛋白质的全部水化补充的水平的样品中，水分子的运动也比在刚性冰晶格中的运动快几个数量级。溶菌酶粉末上的核磁共振松弛数据支持一个模型，该模型使蛋白质表面的吸附水非常流畅，水的重定向关联时间短于纳秒。
Nuclear magnetic resonance (NMR) measurements provide both structural and dynamical information about the molecules in which nuclear resonances are observed. This manuscript addresses NMR relaxation of water protons in protein powder systems. Inclusion of magnetic communication between the water proton spins and protein proton spins leads to a clearer view of water molecule dynamics at the protein surface than has been previously available. We conclude that water molecule motion at the protein surface is somewhat slower than in the solute free solvent, but it is orders of magnitude faster than motions in a rigid ice lattice even in samples hydrated to levels well below what is generally thought to be the full hydration complement of the protein. The NMR relaxation data on lysozyme powders support a model that leaves adsorbed water very fluid at the protein surface with reorientational correlation times for the water shorter than nanoseconds.