Abstract
Characterizing the binding of ligands to macromolecular receptors in solution is important to many areas of chemistry, biology, and nanobiotechnology, but perhaps most notably to drug development. NMR has proven to be particularly useful for such studies, but the systems studied have generally been restricted to model systems with dubious physiological relevance. This paper reviews the use of NMR diffusion measurements to study drug binding and two recent advances that enable measurements to be conducted in more sensitive higher-field NMR spectrometers in non-deuterated aqueous samples.
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25 articles.
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