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DNA binding experiments show that GABPα and CREB preferentially bind the two TFBS when they overlap and produce the ETS⇔CRE motif enriched in proximal promoters.
However, results of limited trypsin digestion and ANS binding experiments show that the backbone structure of the D82R variant is more flexible than that of the wild type hFGF1.
Furthermore, in vitro binding experiments show that Hfq stimulates the base pairing of LhrA to chiA mRNA.
The binding experiments show that the peptides 15D and 15K competitively inhibited chemokine binding to CCR5 (Figure 5A) and CXCR4 (Figure 5B) although with low potency.
In summary, all binding experiments show that the exosome complex of the state A mutant is fully capable of interacting with the cap proteins.
In vitro binding experiments show that the affinity of purified Hfq truncated at residue 66 (Hfq) for binding cfa is similar to that of the wild-type protein; however, the presence of RydC decreases substantially the binding of Hfq.
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However, this model has been largely discounted by in vitro binding experiments showing that purified Ku cannot bind DNA and RNA concurrently (Pfingsten et al., 2012).
Our in vitro binding experiments showed that unlike the homologous DUB USP5, USP13 does not bind ubiquitin with a high affinity.
DNA binding experiments showed that these derivatives behaved as DNA intercalating agents.
Performed DNA binding experiments showed that given Ag(I) species specifically interact with DNA double helix via intercalation and were visualized by confocal microscopy to specifically bind to the nuclei.
Although UMP is the naturally preferred substrate of PolB, the kinetic studies and competitive binding experiments showed that dUMP rather than UMP exhibits higher affinity to PolB (Fig. S7).
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