Braun Daniel, Schmollngruber Michael, Steinhauser Othmar
Department of Computational Biological Chemistry, University of Vienna , Währinger Straße 17, 1090 Vienna, Austria.
J Phys Chem Lett. 2017 Jul 20;8(14):3421-3426. doi: 10.1021/acs.jpclett.7b01013. Epub 2017 Jul 12.
The highly heterogeneous hydration dynamics of protein-water interfaces is considered important for protein stability and dynamics, protein folding, enzymatic activity, and even drug design. The nuclear Overhauser effect (NOE) between protein and water protons is the only experimental observable which, in principle, can provide a map of locally resolved hydration dynamics. However, its utility was questioned in various theoretical studies that emphasized the contributions of long-range NOE interactions. We show by a detailed analysis based on molecular dynamics simulations that, contrary to recent claims, the protein-water NOE is an excellent observable to map local hydration dynamics at the protein surface.
蛋白质 - 水界面高度异质的水合动力学被认为对蛋白质稳定性和动力学、蛋白质折叠、酶活性乃至药物设计都很重要。蛋白质与水质子之间的核Overhauser效应（NOE）是唯一可通过实验观测到的效应，原则上它能提供局部解析的水合动力学图谱。然而，在各种强调远程NOE相互作用贡献的理论研究中，其效用受到了质疑。我们通过基于分子动力学模拟的详细分析表明，与最近的说法相反，蛋白质 - 水NOE是绘制蛋白质表面局部水合动力学的极佳观测指标。
