A major goal in structural biology is to unravel how molecular machines function in detail. To
that end, solution-state NMR spectroscopy is ideally suited as it is able to study biological …

Myriad biological processes proceed through states that defy characterization by
conventional atomic-resolution structural biological methods. The invisibility of these …

It is well-established that dynamics are central to protein function; their importance is
implicitly acknowledged in the principles of the Monod, Wyman and Changeux model of …

Abstract Although Chemical Exchange Saturation Transfer (CEST) type NMR experiments
have been used to study chemical exchange processes in molecules since the early 1960s …

ATP-competitive inhibitors are currently the largest class of clinically approved drugs for
protein kinases. By targeting the ATP-binding pocket, these compounds block the catalytic …

How can a single protein domain encode a conformational landscape with multiple stably
folded states, and how do those states interconvert? Here, we use real-time and relaxation …

Protein–ligand interactions have been commonly studied through static structures of the
protein–ligand complex. Recently, however, there has been increasing interest in …

This review describes off-resonance R 1ρ relaxation dispersion NMR methods for
characterizing microsecond-to-millisecond chemical exchange in uniformly 13 C/15 N …

The prototypical chaperonin GroEL assists protein folding through an ATP-dependent
encapsulation mechanism. The details of how GroEL folds proteins remain elusive …

The fluorine-19 nucleus was recognized early to harbor exceptional properties for NMR
spectroscopy. With 100% natural abundance, a high gyromagnetic ratio (83% sensitivity …