There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.
Abstract
In the half-century since its discovery, nuclear magnetic resonance (NMR) has become
the single most powerful form of spectroscopy in both chemistry and structural biology.
The dramatic technical advances over the past 10-15 years, which continue apace, have
markedly increased the range of applications for NMR in the study of protein-ligand
interactions. These form the basis for its most exciting uses in the drug discovery
process, which range from the simple identification of whether a compound (or a component
of a mixture) binds to a given protein, through to the determination of the full three-dimensional
structure of the complex, with all the information this yields for structure-based
drug design.