Browse our latest Biochemistry and Chemical Biology articles

Structural and biochemical analysis of an abundant and conserved protein complex called EMC shows how it is likely to insert nascent membrane proteins into the endoplasmic reticulum membrane.

An individual extracellular signal regulates multiple cellular actions through differences in the temporal dynamics of spatially distinct populations of the central signaling enzyme, extracellular-signal regulated kinase.

The DNA flanks on either side of an R-loop differ in stability, and CRISPR-Cas12 enzymes form double-strand breaks by targeting the more unstable flank with their single DNase active site.

Sister chromatid cohesion is established during replication by two independent pathways operating in parallel, one converts chromosomal cohesin into cohesive structures while the other loads cohesin onto nascent DNAs.

Both protein-protein and protein-lipid interactions are essential for Rab5 symmetry breaking at the early endosome.

Combined simulations and electrophysiological experiments show that the CLC channels and exchangers form physically distinct and evolutionarily conserved pathways through which Cl^- and H⁺ ions move when crossing biological membranes.

The roles of key telomerase active site residues were elucidated to determine how telomerase selects the correct from the incorrect nucleotide to maintain telomere integrity.

Shifts in the balance between nucleotide-favorable and nucleotide-unfavorable conformations of myosin motors encode duty ratios and ADP release rates, demonstrating the power of an ensemble perspective for uncovering sequence-function relationships.

Researchers should define in advance the criteria for excluding the results of experiments that 'did not work' from articles.

Reconstitution of the endosomal Rab cascade reveals that Rab5 binds and activates the Mon1-Ccz1 guanine nucleotide exchange factor, which in turn recruits Rab7 to membranes to drive fusion.