Sentence examples for most favorable binding from inspiring English sources

A comparison of the binding energy data for the docked poses of vardenafil, tadalafil and IAAP at each of the binding sites (Table S1) suggested that most potent ABCB1 inhibitor, vardenafil, exhibited the most favorable binding energy within the QZ59-RRR binding site of ABCB1, whereas tadalafil interacted most favorably with site-4.

Structure of PDB ID: 2NSD and snapshot conformer at 5.5 ns show most favorable binding with N1 compared to other conformers.

Compound 5 exhibited the best inhibitory activity (pIC50 = 6.36) and most favorable binding free energy (ΔGbind = −47.67 kcal/mol) than other derivatives.

The most favorable binding conformations served as the templates for pharmacophore modeling with Catalyst 4.11 and a virtually generated library have been screened for novel antagonist development.

Molecular modeling and docking studies show that these same AMs have the most favorable binding energies and most close interactions with the molecular model of the SR-A collagen-like domain.

Our results show that among the different commercial drugs, both charged and neutral PAMAM have the most favorable binding free energies for CRO, MTX, and FUS, which appears to be due to a complex counterbalance of electrostatics and van der Waals interactions.

The compound with the most favorable hTK1 binding properties had a kcat/KM value of 57.4% relative to that of thymidine and an IC50 of inhibition of thymidine phosphorylation by hTK1 of 92 μM.

As probed by in-situ and ex-situ spectroscopic techniques and density functional theory, the P=O site of C P=O bonding with the most favorable proton binding energy is identified and associated with highly reversible and fast pseudocapacitive behavior.

It remains unclear if short-range forces could consolidate the interaction with the subset of conformations available that are most favorable for binding the membrane.

In conformational selection, addition of binding partners can result in a population shift in the conformational ensemble of a disordered protein (see section 4.2) toward the conformation that is most favorable for binding.

As shown in Figure 5A, the most energetically favorable binding mode of compound 4b at the active site of AChE comes into a free binding energy of -7.14 kcal/mol.