Protein-water interactions are a fundamental determinant of protein structure and function. Despite their importance, the molecular details of water orientations and dynamics near protein surfaces remain poorly understood, largely due to the difficulty of measuring local water mobility near the protein in a site-resolved fashion. Solution NMR-based measurement of water mobility via the nuclear Overhauser effect was presented as a method for performing comprehensive, site-resolved measurements of water dynamics many years ago. Though this approach yielded extensive insight on the dynamics and locations of waters buried within proteins, its promise for measuring surface hydration dynamics was impeded by various technical barriers. Over the past several years, however, this approach has been pursued anew with the aid of reverse micelle encapsulation of proteins of interest. The confined environment of the reverse micelle resolves many of these barriers and permits site-resolved measurement of relative water dynamics across much of the protein surface. Here, the development of this strategy for measuring hydration dynamics is reviewed with particular focus on the important remaining challenges to its widespread application.

中文翻译：

---

蛋白质水合动力学的综合测量：通过反胶束封装促进基于 NMR 的方法

蛋白质-水相互作用是蛋白质结构和功能的基本决定因素。尽管它们很重要，但蛋白质表面附近的水方向和动力学的分子细节仍然知之甚少，这主要是由于难以以位点解析的方式测量蛋白质附近的局部水流动性。多年前，通过核 Overhauser 效应对基于溶液 NMR 的水流动性进行测量，作为一种对水动力学进行全面的现场分辨测量的方法。尽管这种方法对蛋白质中埋藏的水的动力学和位置产生了广泛的了解，但其测量表面水合动力学的前景受到各种技术障碍的阻碍。然而，在过去的几年里，借助反胶束封装感兴趣的蛋白质，这种方法得到了重新探索。反胶束的密闭环境解决了许多这些障碍，并允许对大部分蛋白质表面的相对水动力学进行现场解析测量。在这里，回顾了这种测量水合动力学的策略的发展，特别关注其广泛应用所面临的重要挑战。