抄録
Life is dynamic and this dynamism is intimately related to the dynamism of protein molecules themselves. The dynamism depends on weak chemical bonding or interatomic potentials, which fluctuate under physiological conditions. By using high pressure NMR spectroscopy, one can explore these fluctuations in atomic details under closely physiological conditions. This paper discusses the manner how high pressure NMR experiments can detect such fluctuations, while conventional NMR spectroscopy fails. The unique nature of the pressure perturbation, as opposed to temperature, is emphasized, which enables exploration, with least perturbation, the subtle nature of such fluctuations, which produce the low-populated, high-energy sub-states of proteins essential for function.
