European Synchrotron Radiation Facilities, 71 Ave des Martyrs, 38000, Grenoble, France.
The Wohl Institute, King's College London, 5 Cutcombe Rd, SE59RT, London, UK.
Chembiochem. 2023 Aug 15;24(16):e202300164. doi: 10.1002/cbic.202300164. Epub 2023 Jul 25.
This review aims to analyse the role of solution nuclear magnetic resonance spectroscopy in pressure-induced in vitro studies of protein unfolding. Although this transition has been neglected for many years because of technical difficulties, it provides important information about the forces that keep protein structure together. We first analyse what pressure unfolding is, then provide a critical overview of how NMR spectroscopy has contributed to the field and evaluate the observables used in these studies. Finally, we discuss the commonalities and differences between pressure-, cold- and heat-induced unfolding. We conclude that, despite specific peculiarities, in both cold and pressure denaturation the important contribution of the state of hydration of nonpolar side chains is a major factor that determines the pressure dependence of the conformational stability of proteins.
本综述旨在分析溶液核磁共振光谱在压力诱导的蛋白质变性体外研究中的作用。尽管由于技术困难，这一转变多年来一直被忽视，但它提供了有关维持蛋白质结构的力的重要信息。我们首先分析了什么是压力变性，然后批判性地概述了 NMR 光谱在该领域的贡献，并评估了这些研究中使用的可观测变量。最后，我们讨论了压力、冷和热变性之间的共同和差异。我们的结论是，尽管存在特定的特殊性，但在冷变性和压力变性中，非极性侧链水合状态的重要贡献是决定蛋白质构象稳定性对压力依赖性的主要因素。
