Monitoring protein folding through high pressure NMR spectroscopy.
 

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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