Solution NMR spectroscopy reveals the energy landscape of immature Cu, Zn-superoxide dismutase and leads to atomic resolution structural models of transiently populated non-native oligomers.

Allostery holds critical role in CRISPR-Cas9 specificity enhancement.

A four-switch long-range allosteric network controls FGF receptor kinase conformational dynamics as well as activity and is applicable to other receptor tyrosine kinases.

Small decreases in pH associated with cellular stress conditions unleash a cryptic mode of client binding in a ubiquitously expressed human small heat shock protein that is more effective at delaying client aggregation.

Internal dynamics play a crucial functional role in MarR (multiple antibiotic resistance repressor) proteins and their role reconciles the distinct allosteric mechanisms proposed previously.

The differential conformational space accessible to the two domains of TRBP, even though they both adopt a canonical dsRBD fold, affect how they interact with target RNAs.

The mechanism of substrate binding cooperativity in human thymidylate synthase does not derive from millisecond dynamic interconversion between active and inactive conformations in solution, but instead results primarily from differential changes in faster side-chain motions (conformational entropy), facilitated by a disordered N-terminus.

The cysteine pair oxidation state in nDsbD acts as a ‘switch’ controlling the presence or absence of frustration in the active-site and determining the dynamic behavior of the cap loop.