Abstract
When a protein exists at equilibrium in more than one conformational state it may be possible to observe separately in the NMR spectrum resonances corresponding to the different states. Provided that interconversion between these states occurs at suitable rates, magnetization transfer techniques may be used to detect it, and in favorable cases to obtain rate constants for specific conformational transitions. Results of one- and two-dimensional 1H NMR experiments with lysozyme and staphylococcal nuclease are used to illustrate the potentials of such an approach to studying the dynamics and folding of proteins.
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