Sentence examples for binding studies indicate that from inspiring English sources

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Aqueous in vitro binding studies indicate that this complex binds to duplex DNA with an affinity of 1.8 × 10 M–1 through a non-classical groove-binding interaction, however, unlike the parent complex [(Ru phen 2)2(tpphz)]4+ (phen = 1,10-phenanthroline), it also displays an increase in MLCT luminescence on addition of liposomes.

The results of our in-vitro binding studies indicate that JDP2 is able to bind DNA either as a homodimer or as a heterodimer with Nrf2 or MafK.

Our binding studies indicate that it is primarily serum Ficolin-3 that binds to acBSA under the experimental conditions used (Figure 2).

DNA binding studies indicate that the isolated C-terminal domain dimer has an interface that binds a single cognate DNA molecule whereas the N-terminal domain is a monomer that also binds a single copy of cognate DNA.

Binding studies indicate that C/EBPα recruitment is weaker in the presence of the C-terminal COP1-binding motif, but the magnitude of this effect suggests that the two bind distinct rather directly overlapping binding sites.

The conformation of the principal epitope is a type I β-turn centered on gp41 residues 664DKW666; in addition, binding studies indicate that residues N- and C-terminal to this core as well as structurally more distant parts of gp41 also contribute to the interaction.

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Whole genome sequencing of spontaneous suppressor mutants capable of robust growth in the presence of lamotrigine revealed mutations in domain II near the N-terminus of initiation factor IF2. Further, in vitro binding studies indicated that lamotrigine binds to IF2 in a nucleotide-dependent fashion and that suppressor mutations abrogated binding.

The anion binding studies indicated that AHP-mB8 has remarkable and specific F− selectivity over other tested anions to exhibit yellow-red color changes for easy naked-eye detection.

The anion binding studies indicated that receptors 6 and 7 comprised of the ferrocene-based benzimidazolium fragment and conjugated group showing better affinity for F− than receptors 4 and 5.

However, previous DNA binding studies indicated that IntI1 has low affinity for the double-stranded attC compared to the bsattC and dsattI1 [12] [14].

Mutational and binding studies indicated that CC and Ex subdomains form a positively charged surface for protein binding.

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