Abstract
Pressure and temperature are fundamental physical parameters to control molecular properties and equilibria of systems. However, pressure approaches to life science are still very limited compared with temperature, due probably to their technical difficulties. Here, nuclear magnetic resonance (NMR) approaches combined with hydrostatic pressure and gas pressure are reviewed. Using NMR spectroscopy with variable pressure is a useful method for characterizing conformational fluctuation of proteins. Gas-pressure NMR spectroscopy using molecular oxygen provides a general and highly sensitive method for detecting internal hydrophobic cavities, which might be sources of protein's conformational fluctuation.
