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These results are consistent with TIG having substantially higher affinity for the bacterial ribosome, broader spectrum of antimicrobial activity and evasion of classic tetracycline-resistance mechanisms and with MIN being more effective than TC as an anti-inflammatory drug.
LD5 showed substantially higher affinity for IgG-F ab' 2, IgG-F ab' 2A than dIgMeither 4L (B3-B3-B3-B3) or SpandwhIgA creathansynergistic didbleither binding sites to the VH3 and Vk regions of the fragment of antigen binding [8].
We also designed and tested another mutant form of CA04/09 HA involving three mutations to make this interaction network hydrophobic (similar to that in SC18 HA) and showed that this mutant (CA04/09mut2) HA had substantially higher affinity than wild-type HA (Figure S3).
Each of the diacyl compounds binds with substantially higher affinity than monoacyl compounds with the same length of acids attached.
Among the Coro1s, Coro1A bound to platelet actin with the lowest affinity with Kd=2.569 μM, whereas Coro1B displayed a substantially higher affinity with a Kd=0.467 μM.
Thus, hagfish insulin would in fact be predicted to have a substantially higher affinity than human insulin if only the classical binding surface was involved.
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For non-DHFR inhibitors such as PMX, RTX, or LMX, polyglutamate derivatives typically show substantially higher binding affinities for intracellular enzyme targets than non-polyglutamylated drugs.
The Alb/58 virus showed dual binding to both α2,6 and α2,3 glycan receptors with its α2,6-binding affinity substantially higher than its α2,3-binding affinity (as observed in dose-dependent direct glycan array binding assay).
This is plausible, because while the DNA affinity of DBD-A DBD-B (~50 nM K DBD-A DBD-Bantially higher than its DBD-A DBD-Bty, those of the individual DBD-A (2 μM K d) and DBD-B (20 μM K d) are not, and as with the intact Rpa heterotrimer, they are thought to associate with and dissociate from DNA sequentially (Arunkumar et al., 2005; Fan and Pavletich, 2012; Fanning et al., 2006).
Interestingly, MCPH1 is able to bind doubly phosphorylated peptides (phosphorylated at Y142 and S139) with its tandem BRCT domains, however its affinity is substantially higher when the substrate is phosphorylated only at S139, whereas MDC1 is unable to bind doubly phosphorylated peptides [104].
Elution profiles of phages modified with specific affinity motifs show substantially higher phage concentration in elution fractions compared to final washing samples.
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