Browse our latest Structural Biology and Molecular Biophysics articles

The time it takes to secrete a protein is dominated by diffusion of positively charged arginines through the channel across the membrane, but lysines avoid this problem as they are neutralised before transport.

Allosteric mechanism of dual β-lactam binding in L,D-transpeptidase from Mycobacterium tuberculosis.

Protein conformational heterogeneity changes upon ligand binding are influenced by ligand properties and can modulate the free energy of binding.

Both the polypeptide and attached O-glycans N-terminal to the A1 domain in von Willebrand factor lower its affinity for its ligand GPIbα on platelets, its stability, and structural dynamics and decrease population of a high-affinity, intermediate state in unfolding.

Designer transmembrane peptides precisely control chimeric antigen receptor signaling strength and are insulated from undesired interactions with endogenous receptors.

The atomic resolution cryo-EM structure of somatostatin receptor 2 (SSTR2) provides insights into the mechanism by which SSTRs recognize their ligands and will serve as a platform to develop selective agonists and therapeutics.

Single particle cryo-electron microscopy associated with functional studies reveal a critical role of N- and C-terminal tails in the autoinhibition of the disease-related ATP8B1-CDC50A lipid flippase, the possible role of phosphorylation in autoinhibition relief, and strong activation by PI(3,4,5)P₃.

Alternative conformations of membrane protein structures can be predicted to high accuracy with AlphaFold2 by reducing the depth of the multiple sequence alignments used for modeling.

An artificial intelligence-based method can predict distinct conformational states of membrane transporters and receptors.

Bacterial warfare protein colicin E1 opens its hinge to plug antibiotic efflux pump TolC and potentiate antibiotics.