Monitoring protein folding through high pressure NMR spectroscopy

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

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Hydrostatic Pressure
  • Kinetics
  • Magnetic Resonance Spectroscopy / methods*
  • Models, Molecular
  • Protein Conformation
  • Protein Folding*
  • Proteins / chemistry*
  • Thermodynamics

Substances

  • Proteins