A new optical tweezers assay sheds light on the mechanism of cooperation and force generation by the subunits of RecBCD, critical for the repair of double strand breaks in bacteria.
Selective import via bacterial ABC importers is facilitated by a hitherto unrecognized complexity in the conformational dynamics of the substrate-binding proteins.
Competition between the antagonistic motor proteins myosin V and myosin VI finely tunes unidirectional transport of cargo on different actin architectures.
New biophysical methods and analyses visualize in real-time a chain of coordinated single-molecular events on a living cell, enabling the inner workings of a mechanoreceptor important to biology to be elucidated.
Small molecule inhibitors identified in a biophysical high-throughout screening assay confirm the importance of the interaction between single-stranded DNA and the protein RAD52 for the survival of BRCA2-depleted cells.
Variability in bacterial transcription start site selection involves DNA “scrunching” and “anti-scrunching,” which may represent a general mechanism for start site selection in all organisms.
The scanning-assisted clustering mechanism of IFI16 not only allows efficient assembly on exposed foreign-dsDNA, but also suppresses the engagement of chromatinized self-dsDNA.
The combined use of optical trapping and single-molecule FRET permits the study of riboswitch structure formation and conformational dynamics at the same time.
Single molecule DNA-binding trajectories and deterministic modeling analyses demonstrate a functional role for high energy partly folded states in Transcription Activator-Like Effectors that could improve future TALEN design.
