期刊
PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
卷 102, 期 -, 页码 15-31出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.pnmrs.2017.05.003
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资金
- French Infrastructure for Integrated Structural Biology [ANR-10-INSB-05-01]
- Roy J. Carver Foundation
- NSF [MCB-1514575]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1514575] Funding Source: National Science Foundation
High-pressure is a well-known perturbation method used to destabilize globular proteins. It is perfectly reversible, which is essential for a proper thermodynamic characterization of a protein equilibrium. In contrast to other perturbation methods such as heat or chemical denaturant that destabilize protein structures uniformly, pressure exerts local effects on regions or domains of a protein containing internal cavities. When combined with NMR spectroscopy, hydrostatic pressure offers the possibility to monitor at a residue level the structural transitions occurring upon unfolding and to determine the kinetic properties of the process. High-pressure NMR experiments can now be routinely performed, owing to the recent development of commercially available high-pressure sample cells. This review summarizes recent advances and some future directions of high-pressure NMR techniques for the characterization at atomic resolution of the energy landscape of protein folding. (C) 2017 Elsevier B.V. All rights reserved.
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