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Prog Nucl Magn Reson Spectrosc. 2017 Nov;102-103:15-31. doi: 10.1016/j.pnmrs.2017.05.003. Epub 2017 Jun 2.

Monitoring protein folding through high pressure NMR spectroscopy.

Author information

1
Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.
2
Department of Biological Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
3
Centre de Biochimie Structural INSERM U1054, CNRS UMMR 5058, Université de Montpellier, Montpellier 34090, France. Electronic address: christian.roumestand@cbs.cnrs.fr.

Abstract

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.

PMID:
29157491
DOI:
10.1016/j.pnmrs.2017.05.003
[Indexed for MEDLINE]

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