Relaxation dispersion spectroscopy is a very powerful NMR method to characterize site-specific thermodynamics and kinetic parameters of chemical exchange processes in proteins on microsecond timescale. This method can also determine chemical shift differences between interconverting states, including low-populated states that are difficult to detect experimentally. A major advantage of the relaxation dispersion spectroscopy over other biophysical methods is that it can provide information on the structure of invisible low-populated states by analyzing the effective transverse relaxation rates of an observable state that interconverts with them. In this review, theoretical and practical aspects of the relaxation dispersion spectroscopy are introduced.
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