Browse our latest Structural Biology and Molecular Biophysics articles

The protofilaments that curl outward from a disassembling microtubule tip carry a large amount of strain energy and they can drive movement with an efficiency similar to conventional motor proteins.

Multiple chaperone binding sites on substrates suggest a mechanism by which the Hsp70 chaperone can circumvent kinetic traps in protein folding.

The structural model of hnRNP A1 shows that it can bind with both RRMs to RNA, which is shown to be relevant for the SMN2 exon 7 splicing mechanism in vivo.

Super-resolution imaging reveals a novel multi-channel arrangement that explains how big potassium (BK) channel activation closely tracks the opening of low-voltage-activated L-type calcium channels.

A combination of genetics and biophysical approaches identifies an overlapping set of sequences that form non-canonical G-quadruplex structures in vitro and induce genomic instability in cells.

Structures of RNA polymerase I transcription machinery revealed a ratcheting motion within the complex in coordination with three distinct functional states, implicating a novel mechanism for promoter bubble opening in the absence of ATP hydrolysis.

Ex vivo characterization of the interaction of human sperm with semen factors reveals that semen amyloids, previously discovered due to their ability to enhance HIV infection, serve a physiological function by promoting disposal of the defective sperm.

A molecular model of the assembled COPI coat, determined by cryo-electron tomography of an in vitro reconstituted budding reaction, reveals details of interactions mediating coat assembly and shows the binding site of ArfGAP2.

Three dimensional reconstructions of the mechanical energy stores of jumping insects reveal how the miniaturized components interact and function.

A novel microscopy-based assay shows that dendritic cells encountering pathogenic stimuli form increased complexes of specific SNARE proteins, driving release of large amounts of inflammatory cytokines.