Affiliation:
1. European Synchrotron Radiation Facilities 71 Ave des Martyrs 38000 Grenoble France
2. The Wohl Institute King's College London 5 Cutcombe Rd SE59RT London UK
3. University Federico II via Cynthia 80110 Naples Italy
Abstract
AbstractThis 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.
Funder
Alzheimer's Research Trust
Subject
Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry