Sentence examples for binding of these ligands from inspiring English sources

A stoichiometry of 1 molecule of ligand per mole of dimeric enzyme was obtained for the binding of these ligands.

Crystal structures of GCPII in complex with various ligands have provided insight into the binding of these ligands, particularly to the S1′ site of the enzyme.

Recently, evidence has provided valuable information on the receptors that mediate these events and the intracellular signaling cascades after the binding of these ligands.

Molecular docking calculation predicted the binding of these ligands in active-site cavity of the CAMKIV structure correlating such interactions with a probable inhibition mechanism.

To perceive the exact mode of binding of these ligands, two models of the ligand EGFR complexes were considered: (1) reversible binding mode in which the ligand had hydrogen bond interactions at the binding site and (2) irreversible binding mode wherein the ligand's Michael acceptor side chain has proximity to the sulfhydryl group of C773 of EGFR, thereby enabling a covalent interaction.

In contrast to results obtained with the peptides alone, co-application of T30 with ACh, MLA, or choline altered binding of these ligands to the α7-nAChR.

Receptor binding experiments confirmed binding of these ligand peptides to their receptors in vitro.

Other types of ligands, e.g., metal ions, may bind to some of the chains, however, the binding sites of these ligands are not considered.

Note that the observed enthalpy (Δ H °obs) for the binding of both these ligands to HDAC8 becomes more favorable (i.e., its negative value increases) with an increase in temperature.

Such analyses indicate that the cationic head of the different compounds must be refined in order to obtain an increase in the binding affinity of these ligands.

An X-ray crystal structure of a bis-ligated iron III) complex, [Fe(SBH m-OMe)(3))(2)]NO(3), confirmSBH m-OMeidonal binding mode of these ligands.