Heterogeneous Preferential Solvation of Water and Trifluoroethanol in Homologous Lysozymes

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• 作者：Evan J. Arthur ; John T. King ; Kevin J. Kubarych ; Charles L. Brooks ; III
• 刊名：Journal of Physical Chemistry B
• 出版年：2014
• 出版时间：July 17, 2014
• 年：2014
• 卷：118
• 期：28
• 页码：8118-8127
• 全文大小：464K
• ISSN：1520-5207

文摘

Cytoplasmic osmolytes can significantly alter the thermodynamic and kinetic properties of proteins relative to those under dilute solution conditions. Spectroscopic experiments of lysozymes in cosolvents indicate that such changes may arise from the heterogeneous, site-specific hydrophobic interactions between protein surface residues and individual solvent molecules. In pursuit of an accurate and predictive model for explaining biomolecular interactions, we study the averaged structural characteristics of mixed solvents with homologous lysozyme solutes using all-atom molecular dynamics. By observing the time-averaged densities of different aqueous solutions of trifluoroethanol, we deduce trends in the heterogeneous solvent interactions over each protein鈥檚 surface, and investigate how the homology of protein structure does not necessarily translate to similarities in solvent structure and composition鈥攅ven when observing identical side chains.