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A single binding site was observed in the BSA rivaroxaban complex and the binding constants indicated that their binding is quite strong to be highly bound in plasma.
The larger values of binding constants indicated that polyamidoamine-C12 25% holds the curcumin strongly.
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Our initial ITC measurements showed variable binding constants, indicating that the purified protein samples might contain different amounts of cAMP (verified by our partial apo structure).
The temperature dependence of the binding constant indicates the induced change in protein secondary structure.
The dissociation constants indicate that Sp1ZF6(Arg)8 has an obvious DNA binding preference to discontinuous target sequences but not Sp1ZF6(Gly)10.
The changes in the chloride ion concentrations of NaCl solutions with initial concentrations of 3.0 mol/L were monitored as functions of time until the solution concentrations were constant, indicating that no further binding was occurring (Thomas et al. 2012).
Comparison of these proteins' in vitro binding sites with their in vivo binding sites indicates that PBM-derived specificitiesificanies caccuratelyely reflect in vivo DNA sequence specificities.
The increase in binding affinity at lower pH was greater for the Ubx optimal binding site than for other DNA binding sites, indicating that subtle sequence alterations in DNA binding sites may influence pH-dependent behavior.
Crystallographically determined, apparent dissociation constants indicated ∼10-fold stronger Na+ binding at pH 8 than at pH 4, consistent with substrate competition for a common ion-binding site.
Conditional stability constant (LogK) and percentages of fluorophores that correspond to metal binding (%f) values indicated that young DOM sample (L-2) had the highest binding affinity to all the three metals ions.
DNA binding constant and molecular model indicated that both the length of linker chain and the distance of interchromophore were key impact factors for DNA binding affinity and biological activity.
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