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Overall, these observations strongly suggest that a large part of EWS-FLI1 DNA binding is driven by GGAA sequence recognition and correlates with genes expression activation through EWS-FLI1 driven long-distance control of transcription.
Thermodynamic parameters suggest that the binding is driven by both enthalpy and entropy, accompanied with only a minor alteration in protein's structure.
It was found that these compounds have higher selectivities for sigma-1 receptors compared to 1. Quantitatitive structure activity relationship studies revealed that sigma-1 binding is driven by hydrophobic interactions.
Here, we exhaustively assess the atomistic binding interactions of this compound with both CCR5 and CXCR4, and we find that binding is driven by π-stacking interactions between aromatic rings on the ligand and receptor residues, as well as electrostatic interactions involving the protonated piperidine nitrogen.
This binding is driven by electrostatic interaction between negative HSPG and five positively charged amino acids [16].
Both cyclic nucleotides bind to the protein through strong enthalpy driving forces, with enthalpy values of −12.5 versus −12.4 kcal/mol at 30°C, suggesting that binding is driven by charge-charge interactions, most likely between the phosphate groups and the highly charged residues of the PBC.
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ITC demonstrated that IgG1 FcγRIIIa binding was driven by favorable binding enthalpy (ΔH) but opposed by unfavorable binding entropy change (ΔS).
The thermodynamic parameters showed that the first-class of binding process was primarily driven by entropy and the second-class of binding was driven by enthalpy and entropy.
The binding was driven by the electrostatic interaction between protonated amines on the dendrimer and SDS at pH ≤ 2.
The active site has been found to be suboptimally hydrated, resulting in ligand binding being driven by enthalpic dispersion forces.
To test if the binding was driven by a single peptide, we used SPR to screen the individual peptides that made up each arm of the synbody against immobilized AKT1.
More suggestions(17)
binding is counterbalanced by
binding is monitored by
binding is dominated by
binding is given by
binding is facilitated by
binding is directed by
binding is inhibited by
binding is increased by
binding is supported by
binding is displaced by
binding is preceded by
binding is explained by
binding is described by
binding is sensed by
binding is measured by
binding is illustrated by
binding is limited by
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