Browse our latest Structural Biology and Molecular Biophysics articles

Cryo-EM studies of doublet microtubules from wild-type and acetylation mutants suggest that acetylation of K40 affects the lateral rotational angle between protofilaments, leading to changes in the structure and stability.

Despite highly conserved sequences, subtle variations in HP1 paralog charge distribution influence distinct liquid-liquid phase separation behaviors, ultimately impacting DNA-mediated heterochromatin organization.

Structural comparison and electrophysiology of OSCA channels shed light on potential structural features influencing response to poke stimulus.

High-resolution NMR data and precise kinase activity assays on Abelson kinase bearing mutations in its αI-helix identify the αI-helix parts involved in disassembly of Abelson’s regulatory core and kinase activation.

Structural insights into the orthosteric inhibition and subtype specificity of P2X receptors by classical P2X antagonists facilitate the rational design of novel competitive antagonists for P2X receptors.

Fibroblast growth factor (FGF) ligands exhibit different preferences for signaling cascades triggered through FGFR1, a receptor which is critical for skeletal development, and these differences likely contribute to the amazing complexity of developmental processes.

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

Thioredoxin functions as a negative allosteric effector of ASK1 by altering the interaction between the thioredoxin-binding and tetratricopeptide repeats domains, thereby reducing access to the kinase domain's activation segment.

The intrinsic disorder of the circadian clock protein Frequency organizes binding partners, facilitates liquid–liquid phase separation, modulates Frequency phosphorylation, and derives from sequence properties conserved with homologous clock components.

Cryo-EM structures uncover glycosylation in the ectodomains of full-length HER4 homodimer and HER2/HER4 heterodimer complexes, revealing how the binding of various growth factors alters dynamics at the dimerization interface.