New spins on protein dynamics from NMR spectroscopy
Frans A.A. Mulder, Ulrika Brath, Mikael Akke, Lewis E Kay

Nuclear spin relaxation provides information on molecular dynamics on time scales ranging from picoseconds to hours with atom-specific spatial resolution. Experiments directed at the amide backbone and methyl side chain dynamics on the picosecond to nanosecond time scale have been developed in the past decades, and have become established methods. Meanwhile NMR has moved into a new time slot, with new methods being developed to report on the microsecond to millisecond time regime. I will discuss these methods, and show examples that illustrate the role of protein dynamics in (i) attaining sparsely populated states that permit ligand access to secluded internal cavites, and (ii) fostering the structural metamorphosis of a small enzyme to accomplish its diverse functions, including peptide bond isomerization and suppression of immune response through the interaction with calcineurin.