NMR Spectroscopy for Monitoring Functional Dynamics in Solution

Abstract

Abstract Protein functional dynamics are defined as the atomic thermal fluctuations or the segmental motions that are essential for the function of a biomolecule. NMR is a very versatile technique that is well suited for obtaining quantitative information from these processes at atomic resolution and in multiple timescales. This article focuses on recent NMR developments to study functional dynamics, making special incidence in the experiments aimed for the characterisation of chemical–conformational exchange in the microsecond to millisecond timescale. In a second section, the novel‐solution NMR techniques that combine chemical exchange with saturation transfer experiments are addressed to finish with an overview on the dynamic information that can be extracted from residual dipolar couplings. Key Concepts NMR is well suited to study biomolecular dynamics at multiple timescales. Many enzymatic reactions occur in the microsecond to millisecond timescale. Relaxation dispersion experiments can extract quantitative information about the exchange process. CEST and DEST experiments provide useful information on conformations that are invisible in the NMR spectrum. Residual dipolar couplings contain information about spin dynamics that can be extracted and quantified.