抄録
Variable-pressure NMR spectroscopy is capable of probing conformational fluctuations of proteins from within the folded structure to nearly the total unfolding with pressure as major variable. It allows one to examine directly the structures of high-energy conformers resulting from thermal fluctuations in atomic detail or at least in residue-specific detail. Some of these conformers are found widely deviated from folded structures in crystals. Importantly, their structures are unique to individual proteins, many of which are apparently designed for function. Furthermore, the self-association reaction of a hen lysozyme mutant forming amyloid protofibrils is shown to be reversible with pressure, suggesting that amyloidosis is also correlated with an intrinsic fluctuation of the protein.
