Abstract
The combination of high-resolution NMR spectroscopy with pressure perturbation, known as variable-pressure NMR spectroscopy or simply high-pressure NMR spectroscopy, is a relatively recent accomplishment, but is now a technique expanding rapidly with high promise in future. The importance of the method is that it allows, for the first time in history, a systematic detection and analysis of structures of high-energy sub-states in proteins along with their equilibrium populations. Here I describe how the method discloses the new concept and roles of proteins in the biological world. Furthermore, I expect that the knowledge on high-energy sub-states of proteins obtained in this way will contribute to a more logical and efficient use of pressure in food and other applications.
