Real-time NMR measurements of protein folding and hydrogen exchange dynamics

Abstract

Results of recent time-resolved NMR spectroscopy project it as one of the more powerful techniques to unravel the structural and dynamical events accompanying polypeptide folding and protein backbone amide hydrogen exchange. It has been possible to interpret the NMR-derived experimental results in the context of energy landscape model of folding and dynamics. Existing methodologies and availability of high resolution spectrometers provide opportunities to address the folding problem by way of a variety of experiments.