NMR Spectroscopy in the Analysis of Protein-Protein Interactions

Protein-protein interactions are a central aspect of biology and NMR spectroscopyis one of the most powerful and versatile methods available to characterizetheir structure, dynamics, kinetics and thermodynamics. In this article, we give anoverview of the suite of approaches available to the researcher who wishes tounderstand their favourite protein-protein interaction in more detail. We beginwith an outline of two fundamental concepts that are important for understandingthe strengths and limitations of NMR spectroscopy – nuclear spin relaxation andchemical exchange. We then present a range of methods including chemical shiftperturbation analysis, nuclear Overhauser effects (and its derivatives), residualdipolar couplings, paramagnetic approaches, solid-state NMR and the analysis oflow-abundance species. Each method is accompanied by recen texamples fromthe literature. Together, these techniques can allow both broad and deep insightinto the mechanistic underpinnings of protein-protein interactions