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Measured log D values for these compounds were typically in excess of 4, and measurement of their plasma protein binding (ppb) revealed that they were highly bound (>99%), leaving only a small free fraction available to bind to the enzyme.
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MM-PBSA calculations revealed that binding was energetically favorable and driven by the electrostatic interactions.
In vitro binding studies revealed that Rio2 binds Slx9-1.
However, a closer look at the binding site revealed that the mutation displaced the side-chains that form the PLP-binding surface (Fig. 3B).
Tissue sections binding assays revealed that Mu-IFN-CSP was also able to specific binding to liver.
DNA-protein binding experiments revealed that cyclic stretch enhanced nuclear binding to the AP-1 site, which was partially supershifted by antibody to c-Jun.
In vitro binding assays revealed that the proper calcium concentration is required for a direct binding of MEKK2 to Lad1.
Quantification of membrane binding revealed that 3Dpol enzyme binds acidic GUVs without a preference for specific acidic lipids (Fig. 4C).
The DNA binding constants reveal that all these complexes interact with DNA through minor groove binding mode.
Further analysis of this binding site reveals that the YopJ binding site is conserved in other MKKs.
Furthermore, the binding kinetics of 15 mutants revealed that binding is regulated by long-range interactions, which can be correlated with the structural rearrangements resulting from peptide binding.
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