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Nuclear Magnetic Resonance is providing atomic resolution insights into various aspects of ligand binding processes. Numerous and very diverse parameters may be measured using NMR to detect molecular binding events, define the structure of the binding site and get detailed information about the driving forces of an interaction. The wealth of experimental strategies that can be used to study a particular system may appear discouraging at a first sight. The aim of this chapter is to provide the reader with the essential concepts and guidelines to undertake NMR studies of protein-ligand interactions and benefit from the unique insights NMR can provide on a given molecular system in solution. After an introduction on the physical principles of NMR, the most efficient methods used to address the who, where and why questions will be described. The range of applications of these methods is discussed and illustrative examples are provided in order to guide the reader during his choice for an appropriate experimental strategy. Practical aspects of these applications are also considered. Finally, the most recent developments of NMR applications that provide mechanistic information about allosteric regulation of binding are given.

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