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With one K+ bound the G-quadruplex was stable, without apparent conformational changes detected till the second K+ beginning binding to the bottom cap at 159.30 ns (Fig. 2D).
Muscle homogenate (1 μg) was incubated overnight at 4 °C to optimize binding to the bottom of 96-well ELISA plates (Santa Cruz Biotech).
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The bottom portion depicts binding of the inhibitor to an allosteric site, competing with substrate activation and producing partial inhibition, and the top portion depicts substrate activation through binding to the allosteric site.
Coupled with opening and closing of FABP4, the ligand may exist in two different binding modes: close to the bottom of the cavity or close to the portal.
In this experiment, a positive sign of the quinate peaks indicates binding to K170M DHQD (bottom spectrum in Figure 6c,d).
Here we are interested in finding the favourable path(s) between incorrect conformational states (ID 9 and 30; states on the edge of the binding funnel) and the best state found by SwarmDock (the state closest to the bottom of the binding funnel; the native complex state).
In the example described below we focus on the properties of the true positive binding funnel and calculate mean first-passage times between distinct conformational states within the funnel, i.e. we are interested in finding the favourable transition path from the top to the bottom of the binding funnel.
While the second K+ ion reached the lower binding site between the bottom and central G-tetrads through the bottom pathway, it bound at 159.3 ns and spent about 5.6 ns to accomplish the binding process.
The T cell bears a surface receptor (T cell receptor, or TCR) that binds to the T cell epitope's amino acid side chains facing upwards, out of the MHC binding cleft, while the MHC binds to the T cell epitope's amino acid side chains facing into "pockets" located on the sides and bottom of the binding cleft.
The sensitivity of AChE to the slender, elongated bisquaternary inhibitor, BW284c51, is due to its bivalent binding via cation-π and π-π interactions to aromatic amino acids of the choline-binding site at the bottom of the gorge and the peripheral site at its rim.
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