Sentence examples for binding of both peptides from inspiring English sources

Although the binding of both peptides was exothermic, the binding of wtEBO16 was slightly more exothermic than the binding of W8A mutant for PC liposomes (Fig. 6A, a and b).

Preliminary screening of the binding of both peptides to the α7-nAChR, when compared with that of acknowledged receptor agonists and antagonists, revealed significant, but incomplete, competition with [125I]α-BTX for receptor binding sites (Fig. 2C).

After 15 min of cellular exposure to the CPPs, weak binding of both peptides to the plasma membrane was observed.

The incorporation of a mini-PEG spacer had no apparent effect on the in vitro properties of the VAP-1 binding peptide; both peptides were stable in plasma incubations and their solubility was very similar.

Moreover, the inhibition of α5 β1 and αv integrins is likely due to the binding of venom peptides, as both lebectin and lebecetin coimmunoprecipitate with these integrins.

As reported for interactions with single acetylation sites in the case of the BRDs of BRD2 (Umehara et al., 2010), alanine mutants of the conserved asparagine (N140 and N443 in the first and second BRDs in BRD4) did also abolish binding of diacetylated peptides in both SPOT assays as well as in ITC.

In addition, we compared binding of peptide-free and peptide-loaded DR1 using an equilibrium sandwich ELISA assay (Fig. 4E).

A sandwich ELISA was used to measure binding of peptide-free or peptide-loaded DR1 to LB3.1 and MEM264 as previously described [22].

As expected for an FxxA site binder in this system, the binding of ATP was not affected by pre-incubation of the protein with 5 c, but 5 c competes with and blocks the binding of both the self-oligomerisation peptide and the Ac-FHTA-NH2 tetrapeptide.

Suboptimal concentration was not able to prevent the non-specific binding of acidic peptides, whereas superoptimal concentration prevented both acidic-peptide and phosphopeptide binding.

Thus, the nature and extent of binding of peptides and proteins, particularly histidine-containing peptides and proteins, is pH-dependent [ 22– 26].