Taking the Escherichia coli TonB transmembrane domain "offline"? Nonprotonatable Asn substitutes fully for TonB His20.

The TonB system of Gram-negative bacteria uses the proton motive force (PMF) of the cytoplasmic membrane to energize active transport of nutrients across the outer membrane. The single transmembrane domain (TMD) anchor of TonB, the energy transducer, is essential. Within that TMD, His20 is the only TMD residue that is unable to withstand alanine replacement without a loss of activity.

The TonB dimeric crystal structures do not exist in vivo.

The TonB system energizes transport of nutrients across the outer membrane of Escherichia coli using cytoplasmic membrane proton motive force (PMF) for energy. Integral cytoplasmic membrane proteins ExbB and ExbD appear to harvest PMF and transduce it to TonB. The carboxy terminus of TonB then physically interacts with outer membrane transporters to allow translocation of ligands into the periplasmic space.

Orientations of overdamped magnetic nanorod-gyroscopes.

Overdamped magnetic nanorod-gyroscopes driven by a rotating magnetic field undergo a series of reorientations when sedimenting on top of a surface in a viscous liquid. By changing the amplitude and the rotation frequency of the driving magnetic field, the nanorod-gyroscope either synchronizes or desynchronizes with the field and rotates either around its long or short axis. The different regimes of motion are explained theoretically by coupling the nanorod-gyroscopes motion to the creeping flow equations of the surrounding fluid.