Sentence examples for most favourable binding from inspiring English sources

Results indicated hydrophobic interactions in the p2 pocket dominated affinity of the most favourable binding ligand (3bl: Ki = 31 nM).

A test series of carbamate analogues were docked into the identified sites to predict the most favourable binding location.

Results suggested that the hydrophobic interactions in the binding pockets of PI3K exploited affinity of the most favourable binding ligands (4c and 4f: inhibitory constant (ki) = 66.22 nM and 107.39 nM).

ΔGPB values show that JMJD2A-tudor-H4K20me2 complex is the most favourable one with a distinct binding free energy of −19,71 kcal/mol [Table 5].

We show that of the three peptides, Ga-Ex4NOD40 and Ga-Ex4NOD12 demonstrate the most favourable in vitro properties and in vivo binding to GLP-1R positive tissue.

Compound 56 was selected for in vivo PK studies, as it had the most favourable in vitro profile (potency, metabolic stability, protein binding, and solubility).

The small organic molecule or peptide used as ligand, binds to its binding site, and the attached polypeptide finds and occupies the most favourable site of interaction on the protein surface in close proximity to the binding site of the small molecule [ 15].

The most favourable substitution produced a second generation inhibitor with a binding affinity for KLK4 similar to that of SFTI-1 for trypsin while selectivity was markedly improved.

This suggests that the binding of MB onto TISW would be least favourable by heterogeneous surface, while the binding of Cd2+ onto TISW would be most favourable by heterogeneous surface (({{0 < 1} mathord{left/ {vphantom {{0 < 1} n}} right. kern-0pt} n} < 1 -favourable, ({1 -favourablet/ {1phantomathord{left/t. kern-0pt} n} > 1)-non favourable).

This class combines a modest subtype binding selectivity with inverse agonism and has the most favourable molecular properties for further lead optimisation towards a central nervous system (CNS) acting medicine.

In purely energetic terms, the common binding site with the decoron monomer is by far the most favourable interaction.