Browse our latest Biochemistry and Chemical Biology articles

Despite the known heme attachment motif (CXXCH) in all c-type cytochromes, attachment elements recognized by human and bacterial cytochrome c biogenesis pathways are distinct, providing clear targets for differential inhibitors.

Biochemical analysis and computational modeling reveal how cells mechanistically control the quality of their proteomes and demonstrate that the precise alignment of subunits in oligomeric complexes can profoundly affect enzymatic properties.

The N-terminal domains enable Lon protease to discriminate and capture selected protein species for degradation by exposed hydrophobic patches and flexible linkages to the hexameric core complex.

A real-time, stopped-flow method, in combination with protein-induced fluorescence enhancement, Förster resonance energy transfer, and time-resolved fluorescence spectroscopy, reveals a kinetic framework for understanding Dicer as a complex molecular motor.

The general transcription elongation factor NusG functions as an intrinsic termination factor in Bacillus subtilis and together with NusA coordinates global gene expression including the motility regulon.

A new way to alter the genome of bacteriophages helps produce large libraries of variants, allowing these bacteria-killing viruses to be designed to target species harmful to human health.

An unbiased mutational screen decodes the molecular basis of phage receptor interactions, identifies key functional regions determining activity and host range, and demonstrates the potential for engineering therapeutic phages.

Heterotrimeric G-proteins can be switched on not only by G-protein-coupled receptors but also by cytoplasmic proteins, resulting in different signaling mechanisms in cells depending on the specific type of activator.

Monitoring SHP2 phosphoproteome dynamics identifies new substrate sites and sites protected from dephosphorylation by its SH2 domains, highlighting distinct scaffolding and catalytic activities in effecting a transmembrane signaling response.

The polymerase activity of PARP1 is converted to hydrolase activity upon binding of Histone Parylation Factor 1 (HPF1) with nucleosome activators.