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Mutations within homeodomains are significant as subtle changes in DNA binding affinity could have important biological affects due to the alteration of downstream gene activation or repression.
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While in vitro binding studies of transcription factors with differential binding affinities could be pursued, it has been well established that computational predictions of binding affinity are highly correlated with experimental measurements [ 56].
In this way, binding affinities could be estimated for compounds as weak as 30 mM.
GABAAR scaffold-binding affinity could be regulated by PKC.
The lack of systematic correlation between the cytokine-induced increase in NIR-conPK specific binding and TSPO expression could have been due to a cytokine-induced increase in the binding affinity of TSPO for PK 11195 and NIR-conPK.
This would provide a binding site for which ZapA could have a much higher affinity.
Such repetitive occurrence of PUF binding sites may affect RNA regulation: different sites could have different affinities for PUF binding leading to dose-dependent or allosteric regulation.
The high affinity could not have been predicted by rational considerations, as the high affinity was associated with a loss of polar interactions and an increased binding entropy.
Our model suggested that replacing the glutamine (prevalent in the north population) for a hydrophobic leucine (prevalent in the south population) could have affected the binding affinity or mtDNA promoter recognition by POLRMT (fig. 4).
Multimeric compounds could have enhanced affinity due to statistical rebinding or simultaneous binding to receptors.
The reduced binding affinity to H3K27me3 in vitro suggests that LHP1-CD* could have compromised activity in vivo.
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