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In acetonitrile, blue shifts in fluorescent emission upon zinc binding are due to the formation of a 1 2 metal/ligand complex, which induced a fluorescent emission at 616 nm at the expense of the fluorescent emission at 672 nm.
The structural changes that occur upon ligand binding are due to intra-subunit rearrangements along the E-F helices and the displacement of interface water clusters.
Likewise, further study is needed to determine whether the two sites that AA-ALIGNER did not predict as imbalanced but that EMSA showed allelic differences in protein binding are due to limitations in AA-ALIGNER or EMSA.
To determine whether the different affinity for nucleic-acid binding are due to specific features of the nucleic acids, EMSA experiments were carried out using increasing protein concentrations and several radiolabelled molecules (RNA, ssDNA and dsDNA), having the same sequence composition.
It is suggested that alterations in protein binding are due to surface "curvature," which can affect two main factors: (i) the orientation, unfolding or distances between adsorbed proteins, and (ii) distortion of the cytoskeleton upon membrane conformation on the shape of the curve [ 302, 328].
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Since this construct lacks the C-μ2 subdomain, it is unable to bind the YxxΦ motif and thus any observed binding is due to nonspecific interactions.
The high antigen binding was due to a site-directed orientation of the thiol-biotinylated fragments.
The reversible binding is due to molecular complementarity between the inhibitor and the active site of hAVCP, which confers the selectivity of the inhibitor.
Preincubation with mAb 7D2 significantly reduced HIV-1NL4-3 binding to IFN-α-treated monocytes comparable to that observed for non-induced monocytes, indicating that IFN-α-induced HIV-1NL4-3 binding was due to Sn alone.
Our results in Fig. 2d indicate that the K472E/R473E mutation per se does not inhibit CAND1 binding, but that decreased CAND1 binding is due to the increased neddylation levels.
The addition of a YB-1 (1 µg) antibody caused a super-shift in the binding product, confirming that binding was due to this transcription factor (Figure 3F, lane 4).
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