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Determining protein small molecule binding affinity is a key component of present-day rational drug discovery.
In fact, CBP binding affinity is a primary determinant of CREB transcriptional activity [38].
It has also been reported that binding affinity is a function of the stability of the ligand-target complex formation and further optimize the new bonds that affect the biological activity of a complex molecule.
According to PDNN, binding affinity is a function of free energy.
Although one-to-one modification between a transcription factor and its binding affinity is a convenient explanation of our observations, it is possible that the mechanisms underlying regulatory motif modification may be more complex in some cases.
Our model is based on the "two-state" approximation (Von Hippel and Berg 1986; Gerland et al. 2002), which assumes the binding affinity is a sum of contributions of opposing amino acid nucleotide pairs, with each contribution being of only two types, "matched" or "mismatched".
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A broad binding spectrum to human enteric viruses with a sufficient binding affinity is an indispensable binding characteristic of EVBP for utilizing it as a virus adsorbent.
This result is consistent with, and complementary of, the findings observed with anti-GXM mAbs 3E5, in that most of the isotype-related contributions to V-region binding affinity are a result of conformational changes on the CH1 domain, rather than CH2 [11].
Both in vivo and in vitro studies of Dscam have revealed that highly specific homophilic binding, which may arise from high binding affinities, is a general property of these cell surface proteins, and that this property is crucial for its proper physiological function [ 1, 4, 20].
Our data provide new insight on the molecular mechanisms of dominant negative activity in RTH and suggest that the inability of mutant TRs to interact with coactivators such as SRC-1, which results from reduced T3-binding affinity, is a determinant of dominant negative activity.
Since lower ATP-binding affinity is a signal of reduced Hsp90α chaperone activity, we speculated that phosphorylation of Hsp90α at these three sites by PKCγ can down-regulate the Hsp90α chaperone machinery.
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