Analysis of conformational changes indicates that activation of acid-sensing ion channels involves protonation of diverse extracellular sites and interaction of interdomain loops with the upper ends of transmembrane helices.

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

A cluster of cofilin along an otherwise bare actin filament induces distinctively asymmetric cooperative conformational changes to the filament on either side of the cluster.

Conformational changes occur within extracellular domain of BCR upon antigen engagement, and these conformational changes are related with the strength of BCR activation and are distinct in IgM- and IgG-BCR.

Crystallography together with electron-resonance spectroscopy, molecular-dynamics simulations, and transport measurements reveal the molecular details of protein conformational change, and how this change contributes to function in a CLC-type chloride/proton exchanger.

Multi-site FRET measurements of moPrP oligomerization at low pH indicate that major conformational changes take place as monomers reversibly transform into large oligomers, which subsequently disassemble reversibly into small oligomers.

Molecular simulations can capture key aspects of the conformational exchange in a protein.

Complexin can have two conformations when bound to a ternary SNARE complex, one of which induces a conformational change of the SNARE complex at the C-terminus.

The characterization of a previously unidentified “outward-facing open” conformational state provides a new framework for understanding the CLC transport mechanism.

Transcriptional activity is characterized for five steroid receptors complexed with multiple ligands and it is shown that the extent of transcriptional activation in complexes is accurately described by conformational shifts in computationally-generated ensembles.