Browse our latest Biochemistry and Chemical Biology articles

Substrate recognition by a receptor protein tyrosine phosphatase is mediated by binding to its pseudophosphatase domain via a short helix that is >100 amino acids distant from the target phosphosite, uncovering principles of phosphatase substrate recognition and potential scaffolding functions.

An atypical configuration of mitochondrial electron transport chain proteins may underlie the exquisite sensitivity of the carotid body to small decreases in oxygen availability.

Three-dimensional structure of CRISPR Cas7-11 shed light on protein evolution and guide development of biotechnology for RNA manipulations in cells.

Molecular dynamics simulations reveal that D-serine competes with glutamate for binding to the NMDA receptor, a finding supported by electrophysiology experiments with consequences for D-serine-focused therapeutic strategies for myriad neurological disorders.

Cyclic peptide natural products didemnin B and ternatin-4 bind the same hydrophobic pocket of eEF1A to inhibit mRNA translation but exhibit kinetic differences that influence rate-limiting conformational changes underpinning aminoacyl-tRNA selection.

A proteo-genomic CRISPR activation screening workflow to accelerate the identification of novel interactions between the secreted and membrane proteome with the potential to define new biological processes and identify future therapeutic targets.

Parkinson’s disease-associated LRRK2 kinase is recruited to membranes by its Rab GTPase substrates, and LRRK2 is both retained on membranes and further activated there by cooperative interaction with the phosphorylated Rab proteins that it generates.

Histone H3 can translocate to the nucleus as a monomer through a pathway governed by importin-5 and transfers to the histone chaperone NASP, having implications in the folding of H3-H4 dimers and, therefore, the kinetics of genome packaging during replication.

A newly discovered pathway suggests histone proteins H3 and H4 are imported into the nucleus as individual units rather than joined together as heterodimers as was previously thought.

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.