2015 年 25 巻 2 号 p. 100-108
We have gained evidence from our high-pressure NMR work on proteins that, unlike in crystals, proteins in solution fluctuate in general in a wide conformational space from within the basic folded (N) even to the fully unfolded (U). Increasing evidence indicates that high-energy sub-states, existing between the two, often have crucial roles in function. Here we find one such example in an enzyme T4 lysozyme, which hydrolyzes the glycosidic bond of the peptidoglycan hetero-polymer of the bacterial cell wall. In this article, we show how we analyze conformational fluctuations of T4 lysozyme in a wide conformational space with high-pressure NMR spectroscopic techniques, from which we identify the high-energy sub-states relevant to function.
