Browse our latest Structural Biology and Molecular Biophysics articles

Cryo-electron tomography reveals how a chaperone protein called TRiC reduces the ability of pathogenic mutant huntingtin proteins to form aggregates.

C-terminal phosphorylation of the lipid phosphatase PTEN drives a reduction in membrane affinity and leads to a more compact conformation that involves a C2 domain-tail interaction.

Quantitative observations of single-molecule binding between antigen and T cell receptor (TCR) in living primary T cells reveals unbinding kinetics, stoichiometry and signaling molecule recruitment, providing insights into the mechanisms of antigen recognition by the immune system.

Computer simulations reveal that viral nucleic acids have an ideal structure for being packaged into outer protein shells called capsids.

Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.

Cryo-electron microscopy has been used to provide a structural interpretation of the complete action cycle of release factor 3 during translation termination, which includes a coordinated sequence of interactions with a class-I release factor and the ribosome.

Charybdotoxin, a toxin produced by scorpions, blocks a K⁺ channel by binding in a lock-and-key fashion to the mouth of the channel and presenting a lysine amino group, which serves as a K⁺ mimic in the selectivity filter.

Experiments on synthetic models of synaptic vesicles have shed new light on the role of the protein α-synuclein in the central nervous system.