Monitoring protein folding through high pressure NMR spectroscopy.
Monitoring protein folding through high pressure NMR spectroscopy.
Prog Nucl Magn Reson Spectrosc. 2017 Nov;102-103:15-31
Authors: Roche J, Royer CA, Roumestand C
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 [PubMed - in process]
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