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IgE binding of the mutant proteins was evaluated by in vitro studies using patients' sera.
The carbohydrate binding of the mutant was markedly impaired compared with that of the wild type and was too weak to allow calculation of a binding constant.
As we mentioned before, FadRWT protein can bind to fadD probe 2 in a dose-dependent manner (Fig. 6B), whereas no significant binding of the mutant protein FadRK113 (wasG) was found (Fig. 6C).
This result could be interpreted in light of the partially impaired binding of the mutant oncoprotein to the GSTP1 molecule.
The result from co-IP experiment indicated a diminished binding of the mutant to HP1 α.
No binding of the mutant DSC2a protein to PG was observed, and binding to PKP2 was unaffected.
Similar(46)
Efficient amplification of stock viruses at 33°C already confirmed the functional receptor binding of the mutants.
When binding of the mutants to lipids was analyzed we did obtain the highest affinity for PC as seen before for pFNR.
We generated single amino acid mutants by replacing each of positions Φ3, Φ4, and Φ5 in hRio2NES with other hydrophobic residues, and tested binding of the mutants to CRM1.
Affinity and specificity of TxA2 binding to the mutant receptor were identical to wild type receptors.
Lastly, in order to quantitatively compare the binding of these mutants to the 60S subunit, we measured the affinities of these mutants to the 60S subunit using Bio-layer interferometry (BLI) (Figs. 3E and S2).
More suggestions(17)
binding of the endogenous
binding of the hydrophobic
binding of the monoclonal
binding of the fluorescent
binding of the second
binding of the secondary
binding of the same
binding of the fatty
binding of the primary
binding of the individual
binding of the active
binding of the extracellular
binding of the natural
binding of the catalytic
binding of the antibiotic
binding of the small
binding of the general
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