Honegger Philipp, Heid Esther, Schmode Stella, Schröder Christian, Steinhauser Othmar
University of Vienna, Faculty of Chemistry, Department of Computational Biological Chemistry Währingerstr. 17 A-1090 Vienna Austria
RSC Adv. 2019 Nov 13;9(63):36982-36993. doi: 10.1039/c9ra08008b. eCollection 2019 Nov 11.
The local changes in protein hydration dynamics upon encapsulation of the protein or macromolecular crowding are essential to understand protein function in cellular environments. We were able to obtain a spatially-resolved picture of the influence of confinement and crowding on the hydration dynamics of the protein ubiquitin by analyzing the time-dependent Stokes shift (TDSS), as well as the intermolecular Nuclear Overhauser Effect (NOE) at different sites of the protein by large-scale computer simulation of single and multiple proteins in water and confined in reverse micelles. Besides high advanced space resolved information on hydration dynamics we found a strong correlation of the change in NOE upon crowding or encapsulation and the change in the integral TDSS relaxation times in all investigated systems relative to the signals in a diluted protein solution.
蛋白质或大分子拥挤效应包封时蛋白质水合动力学的局部变化对于理解细胞环境中的蛋白质功能至关重要。通过分析时间相关斯托克斯位移（TDSS）以及通过对水中单个和多个蛋白质以及限制在反胶束中的蛋白质进行大规模计算机模拟，研究蛋白质泛素不同位点的分子间核Overhauser效应（NOE），我们能够获得限制和拥挤对蛋白质水合动力学影响的空间分辨图像。除了关于水合动力学的高度先进的空间分辨信息外，我们还发现，在所有研究系统中，相对于稀释蛋白质溶液中的信号，拥挤或包封时NOE的变化与积分TDSS弛豫时间的变化之间存在很强的相关性。
