Measuring the Signs of ~1H~α Chemical Shift Differences Between Ground and Excited Protein States by Off-Resonance Spin-Lock R_(1p) NMR Spectroscopy

摘要

Protein dynamics are of fundamental importance for many biological processes, including folding, binding, catalysis, and molecular recognition. Often these dynamics involve conformational rearrangements whereby a highly populated conformer exchanges with one or more low-populated, transiently formed states. Such states can be of functional significance and hence are of interest for detailed study, although their low populations and short lifetimes render them "invisible" to many of the techniques of structural biology.