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To address this apparent inconsistency and further elucidate the relationship between structure and HBGA binding patterns, we performed mutagenesis analysis on the role of the three conserved sites in HBGA binding of the Boxer virus.
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Using the in vitro evolved sequence pattern we performed a bioinformatics analysis to identify potential novel DYNLL-binding proteins.
Using the different overrepresented binding patterns, we constructed an interacting transcriptional network.
To derive the distribution pattern of SYT- SSX2 binding, we performed a sliding window analysis in which each chromosome was subdivided into 500kb bins, and the number of SYT-SSX2 peaks in each bin was tabulated.
To test the binding specificities, we performed ITC to measure the equilibrium disassociation constants (Kd).
To further probe for HNF6 binding activity we performed EMSA band shift assays.
To identify if the present GmPHDs has any DNA binding activity, we performed gel-shift analysis.
To test whether SVOP is a nucleotide binding protein, we performed similar photoaffinity labeling experiments.
To demonstrate that this binding is specific, we performed a competition binding experiment.
To assess the impact of the T109M mutation on PFN1 binding to PLP, we performed molecular-dynamic simulations.
To determine whether β-casein 197 had DNA-binding capabilities, we performed a gel retardation assay.
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