Site-resolved measurement of water-protein interactions by solution NMR.
Site-resolved measurement of water-protein interactions by solution NMR.
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DOI：
10.1038/nsmb.1955
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发表时间：
2011-02
影响因子：
16.8
通讯作者：
中科院分区：
文献类型：
--
作者：
生物大分子与水的相互作用是其结构、动力学和功能的基础。从历史上看，表征溶液中蛋白质水合沃茨的位置和停留时间是相当困难的。限制在反胶束的纳米级内部减缓水动力学，允许使用核磁共振技术检测全球蛋白质-水相互作用。通常由氢交换和长程偶极偶联引起的复杂性被反胶束介质的性质所克服。泛素水合的表征表明，在反胶束内的封装允许检测几十个水合沃茨。在实验室和旋转框架中获得的核Overhauser效应的比较表明，相当大范围的水合水动力学是存在于蛋白质表面上。此外，一个前所未有的集群不同的水合动力学类网站是显而易见的。
The interactions of biological macromolecules with water are fundamental to their structure, dynamics and function. Historically, characterization of the location and residence times of hydration waters of proteins in solution has been quite difficult. Confinement within the nanoscale interior of a reverse micelle slows water dynamics, allowing detection of global protein-water interactions using nuclear magnetic resonance techniques. Complications that normally arise from hydrogen exchange and long-range dipolar coupling are overcome by the nature of the reverse micelle medium. Characterization of the hydration of ubiquitin demonstrates that encapsulation within a reverse micelle allows detection of dozens of hydration waters. Comparison of nuclear Overhauser effects obtained in the laboratory and rotating frames indicate a considerable range of hydration water dynamics is present on the protein surface. In addition, an unprecedented clustering of different hydration dynamic classes of sites is evident.
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影响因子：
6.1
作者：
CONNOLLY, ML
通讯作者：
CONNOLLY, ML
影响因子：
5.6
作者：
LEE, B;RICHARDS, FM
通讯作者：
RICHARDS, FM
影响因子：
4.4
作者：
Halle, B
通讯作者：
Halle, B
影响因子：
2.2
作者：
GRIESINGER, C;ERNST, RR
通讯作者：
ERNST, RR
影响因子：
2.9
作者：
FARROW, NA;MUHANDIRAM, R;KAY, LE
通讯作者：
KAY, LE