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 …

Highlights•Sparsely populated protein states can play significant biological roles.•NMR
spectroscopy can structurally and dynamically characterize 'invisible'protein states.•We …

Membrane encapsulation is frequently used by the cell to sequester biomolecules and
compartmentalize their function. Cells also concentrate molecules into phase-separated …

As structural biology trends towards larger and more complex biomolecular targets, a
detailed understanding of their interactions and underlying structures and dynamics is …

NMR spectroscopy is particularly adept at site-specifically monitoring dynamic processes in
proteins, such as protein folding, domain movements, ligand binding, and side-chain …

Over the last decade amide 15N CEST experiments have emerged as a popular tool to
study protein dynamics that involves exchange between a 'visible'major state and sparsely …

Molecular complexes often sample conformational states that direct them to specific
functions. These states can be difficult to observe through traditional biophysical approaches …

Highlights•NMR yields quantitative data on the dynamics of solution-state protein
structures.•NMR's impact is enhanced by continuous innovation in assignment techniques.• …

Protein function is a consequence of a complex and dynamic equilibrium between
allosterically coupled functional states. However, it is often difficult to distinguish the …

Overwhelming evidence now illustrates the defining role of atomic-scale protein flexibility in
biological events such as allostery, cell signaling, and enzyme catalysis. Over the years …