Pressure and protein dynamism

The dynamism of life depends critically on the dynamism of bio-macromolecules themselves, notably proteins. The bio-macromolecular dynamism originates from weak non-bonding interactions, which inevitably fluctuate under physiological conditions. The fascination lies in the fact that, in proteins, the basically random non-biological fluctuations of atoms are often turned into specific biological fluctuations of larger amplitude, which would be directly coupled to protein function and consequently the dynamism of life such as growth, motility, sensing, adaptation and disease. The success of the combination of pressure perturbation with advanced nuclear magnetic resonance (NMR) spectroscopy by using the online cell method has provided a powerful means for investigating details of such biological fluctuations, which encompass, in general, a much wider conformational space of a protein than hitherto explored. Some representative strategies of high pressure NMR spectroscopy for characterizing protein dynamism will be discussed with actual examples.