Browse our latest Structural Biology and Molecular Biophysics articles

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.

The mechanism of substrate binding cooperativity in human thymidylate synthase does not derive from millisecond dynamic interconversion between active and inactive conformations in solution, but instead results primarily from differential changes in faster side-chain motions (conformational entropy), facilitated by a disordered N-terminus.

Proximity-assisted photoactivation (PAPA) provides a new way to detect protein–protein interactions in single-molecule imaging of live cells.

The isolation of the cell membrane of single cells coupled with AFM enables the study and identification of native membrane proteins in a membrane fragment.

A new binding mode between Rabphilin 3A and SNAP-25 enables efficient SNARE complex assembly via inducing a conformation change in SNAP-25 SNARE motif.

The molecular mechanism that candidalysin uses to perforate membranes is unraveled, which opens the door to the rational design of inhibitors against candidiasis.

Molecular details of the interactions of human Fip1 with CPSF30 and CstF77 unravel key aspects of mRNA polyadenylation and its regulation.

As a Russian doll, mimivirus dsDNA genome is folded in a nucleocapsid-like structure enclosed in the nucleoid compartment, encased in the icosahedral capsid itself decorated by long glycosylated fibrils surprisingly made of the same protein as the genomic fiber.

Cryo-EM and particle classification techniques reveal how the electron-bifurcating [FeFe] hydrogenase from Thermotoga maritima multimerizes to connect distant active sites and reveal different conformational states that enable catalysis.

Structural and biochemical studies explain the topoisomerase V DNA relaxation mechanism by showing that it adopts an unusual conformation when bound to DNA that exposes the active site.