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The binding avidity is the result of multiple cooperative binding interactions with the respective antigen.
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A simple visual inspection of the available empirical frequency distributions of TF-DNA binding plot in log-log scale allows us to suggest that a mixture of at least two distinct skewed sample-size - dependent frequency distributions of binding avidity is present in the data.
One such finding is that cellular receptor binding avidity is an important phenotype that impacts viral fitness (Hensley et al., 2009).
Figure 2C-D Table 3 shows that all empirical distributions of binding avidity are fitted well by the K-W function.
Antibody binding avidity was determined for naturally occurring human antibodies against the C-terminal recombinant proteins from MSP3-family members using dot-blot assay.
Our data demonstrates that artificial multiple tandem human IgA affibodies with relevant biological binding avidity were successfully yielded by phage-based molecular evolution.
Nevertheless, it was reported that multivalent binding avidity can be kinetically limited if the binding affinity of an individual receptor-ligand pair is too tight [44, 45].
Naturally, TF-DNA binding avidity could be quantified by the number of TF molecules binding a given specific locus including specific binding element(s) and its flanking regions.
By measuring the relative avidity of anti-Hcβtre serum Ig with the use of a modified ELISA [29] [31] that tests serum at similar antibody concentrations, we determined that serum samples with BoNT/A neutralization activity exhibited a relative binding avidity that was significantly higher than the relative avidity of non-neutralizing antibodies.
We have already demonstrated that a "dimer binding to dimer" scenario providing avidity is such a factor, which can increase apparent affinity by several orders of magnitude [20].
Only pulled-down TF-DNA complexes containing DNA fragments with maximal relative binding avidity could be reliably detected.
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