The first-in-class kinase inhibitor, Ibrutinib, destabilizes its autoinhibited Bruton’s tyrosine kinase (BTK) target, and a remote resistance mutation causes global structural changes that activate BTK catalytic activity.

Hydrogen-deuterium exchange mass spectrometry reveals nucleotide-driven conformational regulation of Sec protein-channel to help impose directionality for protein transport through the Sec complex.

An in-depth binding profile analysis of BRAF domains related to RAF activation and autoinhibition unveils the distinctive roles of each domain in selecting preferred RAS isoforms and facilitating autoinhibition.

SARS-CoV-2 spike protein binding to receptor angiotensin-converting enzyme 2 allosterically enhances furin proteolysis at distal S1/S2 cleavage sites.

Both the polypeptide and attached O-glycans N-terminal to the A1 domain in von Willebrand factor lower its affinity for its ligand GPIbα on platelets, its stability, and structural dynamics and decrease population of a high-affinity, intermediate state in unfolding.

The utilization of hydrogen/deuterium exchange mass spectrometry reveals dynamic insights and interactions driving liquid-liquid demixing of the chromosome passenger complex.

The first structural and biochemical study of the role of the ATP-cone in anaerobic ribonucleotide reductases shows that dATP allosterically prevents transfer of a glycyl radical to the substrate.

Lab-evolved 'super Spy' chaperones show enhanced flexibility, which allows them to bind to and stabilize proteins more effectively than natural chaperones.

Unique methodology was used to generate a large HDX-MS dataset to inform ligand-mediated activation of RORγ, an approach that can be extended to other nuclear receptors with unresolved ligand-dependent activities.

Pulsed-labeling hydrogen exchange on the ribonuclease H family show that the major folding intermediate is conserved over three billion years of evolution, but the path leading to this intermediate varies.