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By random nonstandard peptide integrated discovery, combinatorial macrocyclic peptides were leavaged that target a heterodimeric ABC transport complex and explore fundamental principles of the substrate translocation cycle.

Cryo-EM structures reveal the structural dynamics of ArfA*RF2-mediated rescue of stalled ribosomes.

A structural investigation reveals details of the mechanism by which the nuclease RecJ processes DNA ends to repair double strand breaks.

Stochastic mRNA and non-coding RNA hybridisation has a major impact on protein expression.

Salinamide A exerts antibacterial activity by binding to the bridge-helix cap of bacterial RNA polymerase and allosterically inhibiting nucleotide addition

Protein disaggregases employ two mechanically-linked ATPase rings that are under steric control by a wrapped-around coiled-coil belt.

Co-evolving residue pairs in the different components of a protein complex almost always make contact across the protein–protein interface, thus providing powerful restraints for the modeling of protein complexes.

A parsimonious biophysical model correctly predicts the conserved expression stoichiometry of core bacterial mRNA translation factors, providing intuitive and quantitative design principles for in vivo pathway construction.

Single-molecule F₁F_O studies show mutation-dependent pKa changes of both F_O half-channels, and proton translocation-dependent 11° ATP synthase-direction sub-steps, which support a Grotthuss proton transfer-dependent two-step F_O torque generating mechanism.

Nuclear magnetic resonance analysis revealed the structural and dynamical changes in MgtE during the channel closure caused by the cooperative Mg²⁺-binding, which had remained undescribed only by a static crystal structure.