Water-mediated interaction at a protein-protein interface
Water-mediated interaction at a protein-protein interface
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DOI：
10.1016/j.chemphys.2004.05.010
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发表时间：
2004-12-27
期刊：
影响因子：
2.3
通讯作者：
Ito, N
中科院分区：
文献类型：
--
作者：
Ikura, T;Urakubo, Y;Ito, N
利用表面等离子体共振和低温X射线晶体学研究了芽孢杆菌RNA酶与芽孢杆菌RNA酶抑制剂之间的水介导的间接相互作用。在pH7.4和25 ℃条件下，在150 mM NaCl存在下，芽孢杆菌RNA酶抑制剂D35 A、D39 A、E76 A和E80 A的四个酸性残基的突变分别使结合自由能降低17.2、25.2、3.8和2.1 kJ mol（-1）。由突变引起的复合物的水合结构的变化局限于突变位点周围，表明结合自由能的差异与局部水合结构的差异密切相关。然后，平均结合自由能估计为4.4 kJ mol（-1）每个水介导的间接相互作用的基础上的氢键网络的差异。(C)2004 Elsevier B. V.保留所有权利。
The water-mediated indirect interaction between barnase and barstar was investigated by surface plasmon resonance measurement and cryogenic X-ray crystallography. Mutations of four acidic residues of barstar, D35A, D39A, E76A and E80A, decreased the binding free energies by 17.2, 25.2, 3.8 and 2.1 kJ mol(-1), respectively, in the presence of 150 mM NaCl at pH 7.4 and 25 degreesC. The changes of the hydrated structures of the complexes caused by the mutations were localized around the mutational site, suggesting that difference in the binding free energy is closely correlated with difference in the local hydrated structure. Then, the averaged binding free energy was estimated at 4.4 kJ mol(-1) per water-mediated indirect interaction on the basis of the difference in hydrogen bonding network. (C) 2004 Elsevier B.V. All rights reserved.