The clinically approved BTK kinase active site inhibitors alter the conformational equilibrium of full-length BTK in distinct and unexpected ways.

A novel pair of isobaric crosslinking reagents is described, which allow relative quantification of crosslinker-modified peptides during mass spectrometry analysis for comparative structural studies of proteins and protein complexes.

Multiple lines of evidence demonstrate that a single N-glycan on one receptor influences the strength of a cytotoxic response elicited by natural killer cells following stimulation with an antibody-coated target.

LptC regulates the LPS entry gate in LptB₂FG, likely through a dynamic behavior of its transmembrane helix, while the β-jellyroll domains are tethered in the periplasm.

The dynamical transition between a protein and its surface water is decoupled.

Structure-function analysis reveals an allosteric mechanism activating a plant immune receptor kinase 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.