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

Results of recent time-resolved NMR spectroscopy project it as one of the m ore powerful techniques to unravel the structural and dynamical events acco mpanying polypeptide folding and protein backbone amide hydrogen exchange. It has been possible to interpret the NR;IR-derived experimental results in the context of energy landscape model of folding and dynamics. Existing me thodologies and availability of high resolution spectrometers provide oppor tunities to address the folding problem by way of a variety of experiments.