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.
Hydrogen-Deuterium exchange experiments show that Ric-8A induces similar dynamic changes in the structure of Gα as G protein-coupled receptors, yet protects a larger surface of the nucleotide-binding Ras domain.
The lipid kinase VPS34 complexes I and II are both activated by unsaturation of substrate and non-substrate lipids, curvature, electrostatics and polyphosphoinositides, which play roles in localisation and cellular function.
Client protein-driven reversal of endoplasmic reticulum chaperone (BiP) mediated-repression is revealed as a principal component of the regulation of the unfolded protein response transducer IRE1 in cells.
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.