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.

How the process of protein folding may be controlled by the Sec machinery to assist protein transport across membranes.

Heat-induced local unfolding allows Hsf1 to form trimers and bind to DNA, which depends on Hsf1 concentration and is promoted, not inhibited, by Hsp90.

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.

Understanding the complex auto-regulatory mechanisms for guanine nucleotide exchange factors is critically important for fully appreciating the layers of control for small GTPases.

Atomic details on structural organization and conformational dynamics of the key regulator of neuronal signaling shed light on its allosteric regulation and role in regulating cellular pathways.

A Caenorhabitis elegans RNA-binding protein, FBF-2, modulates RNA sequence motif recognition through conformational change and partner protein interaction.

ER-resident chaperones and cargo receptors make excursions to the cell surface and endocytic compartments when they accompany misfolded clients to lysosomes for degradation.

First experimental studies on the ion atmosphere around a nucleosome provide a quantitative analysis of the molecule's electrostatic properties.