High-Pressure NMR for Studying Protein Structure and Dynamics

doi:10.11938/cjmr20160101

Abstract

Abstract:

Proteins are thermodynamic entities that exist in general as an equilibrium mixture of the basic folded states, denatured states and various intermediate states with varying populations at certain temperature and pressure. When using pressure as a perturbation, the population will be scanned from the states with larger partial molar volumes to the states with smaller ones. Therefore, high-pressure NMR is applicable to study protein structure and dynamics at wider conformational space at the atomic level. Furthermore, under physiological conditions, the difficulty of detection of higher-energy substates by the conventional NMR is obvious, as the equilibrium populations of such higher-energy substates are extremely low. Hydrostatic pressure gives a general solution to this problem. The partial molar volumes of proteins at higher-energy states, being functionally relevant most of the time, are generally smaller than those at the basic folded ones, therefore, pressure can shift the equilibrium toward the former substantially, and allows their detection at elevated pressure. Recently, owing to the development of the high pressure NMR and multidimensional NMR technologies, and substantial development of protein structure and dynamics study itself, high pressure NMR spectroscopy is being paid more and more attention. In this review, the history, concepts, techniques, and applications of high-pressure NMR are presented with future prospects.

Key words: high-pressure NMR, protein structure, protein dynamics, partial molar volume, volume fluctuation, low-lying excited state

CLC Number:

O482.53

LI Hua, Yuji O. KAMATARI, Ryo KITAHARA, Kazuyuki AKASAKA. High-Pressure NMR for Studying Protein Structure and Dynamics[J]. Chinese Journal of Magnetic Resonance, 2016, 33(1): 1-26.

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