New Views of Functionally Dynamic Proteins by Solution NMR Spectroscopy

In the past several decades solution NMR spectroscopy has emerged as a powerful technique for the study of the structure and dynamics of proteins, providing detailed insights into biomolecular function. Herein, I provide a summary of two important areas of application, focusing on NMR studies of (i) supramolecular systems with aggregate molecular masses in the hundreds of kilodaltons and of (ii) sparsely populated and transiently formed protein states that are thermally accessible from populated ground-state conformers. The critical role of molecular dynamics in function is emphasized, highlighting the utility of the NMR technique in providing such often elusive information. [Display omitted] •Recent advances in solution NMR spectroscopy have led to new avenues for study, focusing on functional dynamics of molecular machines and characterization of rare conformational states of proteins.•Concrete examples of use of solution NMR spectroscopy to study high-molecular-mass systems and rare conformational states are described.•Atomic-resolution characterization of dynamic processes in biomolecules provided by NMR will be potentiated through complementary experimental studies involving X-ray crystallography, cryo-electron microscopy and computational studies.•Current challenges in the field are discussed.