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The bilayers were found to be strongly adhesive and able to prevent platelet binding.
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The lateral mobility of fluorescently labeled lipids fused into solid-supported bilayers is found to change upon deposition on the membrane surface of an amphipathic alpha-helical peptide (AH) derived from the hepatitis C virus (HCV) NS5A protein.
From a static point of view, the proteins embedded at low 50% density in the fluidic lipid bilayer were found to be loosely distributed over the membrane at any instant during the observation.
However, the effect of γ0 and ω on the roughness of the interface of (PS-mCOOH /(PS-mCOOH /bilayer is found to be quite different.
The first bilayer is found to show rather different physico-chemical characteristics as compared to the subsequent bilayers, and this is attributed to the difference in the adsorption environments.
Compared to dipalmitoyl-phosphatidylcholine (DPPC), the electroporation threshold for the bilayer was found to increase from ~ 2 V to 4.3 V at 323 K, and to 5.2 V at 298 K.
The diffusion coefficient (D) of the lipid bilayer was found to be 4.1 μm/s.
The Ka determined from the nonlinear least-squares fit to eq 4 for PnA binding to a 5 mol % GM1-doped DOPC bilayer was found to be (5.4 ± 0.7) × 10 M–10
Measurements have been performed in microstrip line based test fixture where first real and imaginary parts of complex relative permittivity have been obtained, then the refractive index is used to estimate the phase velocity in single and bilayer graphene, this index were found to be higher at lower frequency below 1.5 GHz.
For example, in two studies, the association constants of model transmembrane helices were found to be 100-fold stronger in lipid bilayers than in detergent micelles.
Voltage-gated sensors in the K+-channels HsapBK and KvAP were found to form an α-helix on the bilayer surface.
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