Structural mass spectrometry reveals conformational changes in emerging SARS-CoV-2 spike protein variants that correlate with increased viral fitness.

Multiple iso-energetic-specific interactions involving the intrinsically-disordered region of sHSP HSPB1 define a quasi-ordered state, providing insights into inherited disease-associated mutations within the region that are thought to be disordered.

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

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

A new class of antibody binding a highly conserved epitope on the spike S2 domain of MERS-CoV, SARS-CoV, and SARS-CoV-2 viruses is described.

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.

Multiple dynamic protein interactions converge to regulate the catalytic activity of the B cell kinase, BTK.

The central RNA interference protein, human Argonaute-2, releases its target following phosphorylation on a critical loop in the protein, freeing microRNA-bound Argonaute-2 to seek out and repress additional targets.

A combination of X-ray crystallography, NMR, and mass spectrometry has revealed how diverse small-molecule inhibitors bind Bruton’s tyrosine kinase and alter the conformation of this enzyme.

Molecular architecture of the secreted NS1 dimer from dengue virus infection in complex with a high density lipoprotein particle.