Tompa Kálmán, Bokor Mónika, Ágner Dorina, Iván Dávid, Kovács Dénes, Verebélyi Tamás, Tompa Péter
Institute for Solid State Physics and Optics, Wigner Research Centre for Physics, Hungarian Academy of Sciences, H-1122, Budapest, Konkoly-Thege út 29-33., Hungary.
Department of Physics, Faculty of Natural Sciences, Budapest University of Technology and Economics, H-1521, Budapest, Budafoki út 8., Hungary.
Chemphyschem. 2017 Mar 17;18(6):677-682. doi: 10.1002/cphc.201601136. Epub 2017 Feb 7.
In this work the groundwork is laid for characterizing the mobility of hydrogen-hydrogen pairs (proton-proton radial vectors) in proteins in the solid state that contain only residual water. In this novel approach, we introduce new ways of analyzing and interpreting data: 1) by representing hydrogen mobility (HM) and melting diagram (MD) data recorded by wide-line H NMR spectroscopic analysis as a function of fundamental temperature (thermal excitation energy); 2) by suggesting a novel mode of interpretation of these parameters that sheds light on details of protein-water interactions, such as the exact amount of water molecules and the distribution of barrier potentials pertaining to their rotational and surface translational mobility; 3) by relying on directly determined physical observables. We illustrate the power of this approach by studying the behavior of two proteins, the structured enzyme lysozyme and the intrinsically disordered ERD14.
在这项工作中，我们为表征仅含有残余水的固态蛋白质中氢-氢对（质子-质子径向矢量）的迁移率奠定了基础。在这种新方法中，我们引入了分析和解释数据的新方法：1）通过将宽线H NMR光谱分析记录的氢迁移率（HM）和熔化图（MD）数据表示为基本温度（热激发能）的函数；2）通过提出一种对这些参数的新解释模式，揭示蛋白质-水相互作用的细节，例如水分子的确切数量以及与其旋转和表面平移迁移率相关的势垒分布；3）通过依赖直接测定的物理可观测量。我们通过研究两种蛋白质（结构酶溶菌酶和内在无序的ERD14）的行为来说明这种方法的威力。
