Mapping the hydration dynamics of ubiquitin.
Mapping the hydration dynamics of ubiquitin.
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DOI：
10.1021/ja202033k
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发表时间：
2011-08-17
影响因子：
15
通讯作者：
Wand, A. Joshua
中科院分区：
文献类型：
--
作者：
Nucci, Nathaniel V.;Pometun, Maxim S.;Wand, A. Joshua
水与蛋白质等生物分子相互作用的性质很难在原子分辨率下进行详细研究。溶液核磁共振波谱可能是一种表征蛋白质水合结构和时间方面的强大方法，但一直受到伪影的困扰。将感兴趣的蛋白质封装在反胶束颗粒的水性核心内，导致水动力学普遍减慢，氢交换化学显着减少，并消除大量水的贡献，从而能够利用核奥弗豪瑟效应来量化蛋白质表面和水合水之间的相互作用。在这里，我们扩展了这种方法，以允许使用水合水和与蛋白质碳原子键合的氢之间的偶极相互作用。通过使用低粘度液体丙烷来控制反胶束粒子的分子重新取向时间，与 13C 键合的 1H 的 T1ρ 弛豫时间常数被充分延长，从而获得高质量的旋转框架核欧沃豪塞效应。这些数据补充了先前从蛋白质和与氮键合的氢之间的偶极相互作用获得的结果，并且总体覆盖了蛋白质的大部分分子表面。观察到了广泛的水合动力学。还可以看到分子表面上水合动力学的聚集。长寿命水合水的区域与参与结合配偶体分子识别的蛋白质区域相对应，这意味着溶剂熵对结合熵的贡献已通过进化最大化。
The nature of water’s interaction with biomolecules such as proteins has been difficult to examine in detail at atomic resolution. Solution NMR spectroscopy is potentially a powerful method for characterizing both the structural and temporal aspects of protein hydration but has been plagued by artifacts. Encapsulation of the protein of interest within the aqueous core of a reverse micelle particle results in a general slowing of water dynamics, significant reduction in hydrogen exchange chemistry and elimination of contributions from bulk water thereby enabling the use of nuclear Overhauser effects to quantify interactions between the protein surface and hydration water. Here we extend this approach to allow use of dipolar interactions between hydration water and hydrogens bonded to protein carbon atoms. By manipulating the molecular reorientation time of the reverse micelle particle through use of low viscosity liquid propane, the T1ρ relaxation time constants of 1H bonded to 13C were sufficiently lengthened to allow high quality rotating frame nuclear Overhauser effects to be obtained. These data supplement previous results obtained from dipolar interactions between the protein and hydrogens bonded to nitrogen and in aggregate cover the majority of the molecular surface of the protein. A wide range of hydration dynamics is observed. Clustering of hydration dynamics on the molecular surface is also seen. Regions of long-lived hydration water correspond with regions of the protein that participate in molecular recognition of binding partners implying that the contribution of the solvent entropy to the entropy of binding has been maximized through evolution.
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影响因子：
4.4
作者：
Halle, B
通讯作者：
Halle, B
DOI：
10.1073/pnas.0606235103
发表时间：
2006-09-19
影响因子：
11.1
作者：
Qiu, Weihong;Kao, Ya-Ting;Zewail, Ahmed H.
通讯作者：
Zewail, Ahmed H.
影响因子：
8
作者：
Tanford, C
通讯作者：
Tanford, C
影响因子：
16.6
作者：
EIGEN, M
通讯作者：
EIGEN, M
影响因子：
2.8
作者：
BRUSCHWEILER, R;WRIGHT, PE
通讯作者：
WRIGHT, PE