Monitoring protein folding through high pressure NMR spectroscopy

摘要

Graphical abstractDisplay OmittedHighlights?The use of Hydrostatic High Pressure to unfold Proteins is discussed.?The benefits of combining High-Pressure with NMR to analyze the unfolding reaction are demonstrated.?Recent technological and methodological improvements in HP NMR are presented.?Possible further developments of the method are discussed.AbstractHigh-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