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To explore hexagon diffusion on the membrane surface, fluorescence recovery after photobleaching (FRAP) was performed.
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This fouling phenomena blocked the membrane surface for fluorescence readings.
As the PBsome complexes diffuse upon the membrane surface, one should observe: (1) a fluorescence loss in the unbleached area if the PBsomes diffuse across the cells (Figure 4A C); (2) successive flattening of the slope of the fluorescence intensity gradient (Figure 4A C); (3) changes of the recovery rate as a function of distance from the edge of the bleached area (Figure 4D F).
There was also an accumulation of fluorescence on the membrane surface of individual IPCs that suggests probable reactivity against tissue component.
Surface Plasmon field-enhanced Fluorescence Spectroscopy (SPFS) was used to concurrently measure Aβ adsorption to the membrane surface, the avidity of these interactions and the fluorescence flux through the permeated membranes [15], [26].
We interpret this as the quenching of the Alexa568 fluorescence as the JM peptides aggregate on the membrane surface.
The fluorescence intensity of the label fluorophore was measured on the membrane surface and for the collected flow through.
The lower membrane surface was fixed by 4% formaldehyde, stained with Hoechst 33 342 and counted under a fluorescence microscope.
Small-molecule CXCR4 antagonist AMD3100 (300 nM) inhibited the SDF-1-triggered receptor internalization, which was indicated by the diffuse pattern of the EGFP-CXCR4 fluorescence indicative of the presence of the receptor on the cell membrane surface.
15N-NMR spectroscopy, depth-dependent fluorescence quenching, CD-spectroscopy experiments, and MD simulations indicate a helix orientation of K∗ parallel to the membrane surface.
Peptide-induced membrane permeabilization follows binding to the membrane surface.
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