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Computational and theoretical models reveal mechanisms by which protein compartments assemble around enzymes and reagents to facilitate reactions in bacteria, allowing the identification of strategies for reengineering such compartments as customizable nanoreactors.

Integration of complementary computational approaches reveals an evolutionarily conserved interaction interface between molecular chaperones Hsp70 and Hsp40, rationalizing previous observations.

The role of an important gating domain in linkage between the benzodiazepine drug-binding site and the pore gate in GABA_A receptors.

The architecture of the bacterial cytokinetic ring in cells and in artificial liposome reconstitutions has been described using electron microscopy, leading to a mechanism of constriction.

Lactic acid bacteria engage a hybrid metabolism which blends features of fermentation and respiration when they perform extracellular electron transfer.

A naturally-occurring small molecule acts as a chemical chaperone in vivo to alter the folding of a budding yeast septin and promote an oligomerization pathway that was lost during evolution.

Malaria parasites target a polyprenyl synthase enzyme to the apicoplast organelle and require its activity to produce long-chain linear isoprenoids necessary for apicoplast biogenesis.

A rapid absorption and retention of antimicrobial peptides by dead Escherichia coli cells can increase the survivability of the cell population in a "cooperative" fashion.