Browse our latest Structural Biology and Molecular Biophysics articles

Cryo-electron tomography of COPI vesicles in the Golgi reveals coat structure, disassembly dynamics, cargo binding, and morphological variability.

Single-molecule measurement of conformational dynamics using a genetically encoded fluorescent probe suggests that the selectivity filter region of TRPV1 channels undergoes dynamic motion during agonist activation.

Advances in imaging techniques have shed new light on the structure of vesicles formed by COPI protein complexes.

X-ray crystallographic studies have completed the first atomic resolution description of the kinetic cycle of a potassium channel's pore domain.

The ability of lipid nanodiscs to trap different types of amyloid intermediates, as successfully demonstrated in this study for human-IAPP, could become one of the most powerful approaches to dissect the complicated misfolding pathways of protein aggregation.

Molecular simulations show how hydrophobicity and conformational disorder underlie the phase separation of elastin-like peptides and the elasticity of human tissues.

ER-stress sensing mechanism of the unfolded protein response sensor/transducer IRE1 is conserved from yeast to mammals, where in mammals, unfolded protein binding to IRE1's ER lumenal domain is coupled to its oligomerization and activation through an allosteric conformational change.

Vertebrate superfast muscles employ similar excitation–contraction strategies but distinct myosin heavy chain genes to allow superfast performance, revealing a maximum speed that cannot be overcome without sacrificing neural control.

Allostery in an intrinsically disordered domain of glucocorticoid receptor is mediated by opposing thermodynamic signals that are directed through the production of different isoforms.

A disordered region at the N-terminus of the glucocorticoid receptor can fine tune how cells respond to a hormone via an allosteric mechanism.