Exact(54)
In the closed vicinity of a single nanopore inserted in a lipid membrane, whose electric potential on the trans side is negatively biased, the trans-added negatively charged bacteria are electrophoretically driven towards the lumen entrance of the protein by the electric field lines generated by the transmembrane potential.
A voltage of 600 mV is applied on the trans side.
The polyanions are significantly more effective at reducing the conductance when added to the trans side of this channel.
The negative electric potential on the trans side of a lipid membrane containing a single α-HL nanopore drives negatively charged bacteria into the nanopore.
Control experiments performed in the absence of bacteria, or in the presence of bacteria added on the trans side, but positively biased membranes, confirmed the absence of such blockade events (Additional file 1: Figure S1).
As presented above, to explain this apparent paradox, we note that the entrance of the α-HL's β-barrel lumen, pointing towards the trans side, is negatively charged at neutral pH [53].
Similar(6)
Binding of a ligand to Notch could thus result in a trans, side-by-side interaction, overlapping the two membrane-bound molecules and thus bringing two neighboring cellular membranes into close apposition.
Similar to the above discussion, trans-acceleration in GLUT1 can be explained by the fact that k −2 ≫ k 4, given the argument that, once the second substrate is added on the trans-side, the rate-limiting step switches from the k 4 step to the k −2 step in the King Altman plot.
Membrane conductance was measured by two Ag/AgCl electrodes on the cis- and trans-side of the membrane.
After a stable bilayer was obtained a small amount of oligomeric protein (final concentration 200 nM) was added to the solution on both the cis- and trans-side of the membrane and the solution was thoroughly mixed.
Myosin VI is present in vesicles at the Golgi complex that are on average 200 400 nm away from the trans-side of the Golgi complex [52,53].
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