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The binding interactions of compounds with high binding affinity to Bcl-2 protein were analyzed.
Molecular docking has predicted the plausible binding interactions of compounds 3f, 3g and 3j with α-glucosidase.
Docking simulations predicted key binding interactions of compounds with BChE and CaE and revealed that the best docked positions in BChE were at the bottom of the gorge in close proximity to the catalytic residues in the active site.
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Furthermore, the binding interactions of compound 7k with α-glucosidase was confirmed through molecular docking.
Furthermore, the binding interactions of compound 7e with the active site of α-glucosidase were confirmed through molecular docking.
We investigated the binding interactions of compound 28 by an enzyme ligand molecular modeling (docking) studies, which showed favorable binding interactions in both COX-2 and 5-LO Xactive sites.
The binding interactions of compound 14 with bovine serum albumin demonstrate that hydrogen bonds and van der Waals forces play important roles in the strong association of compound 14.BSA.
The molecular docking analysis was performed to understand the binding interactions of these compounds to COX-2 enzyme.
In addition, strong binding interactions of the compounds with the amino acid residues were effective for the successful identification of α-glucosidase inhibitors.
Docking simulations enabled the detection of key binding interactions of the compounds with AChE and revealed that they occupied mainly the catalytic active site.
Moreover, molecular docking studies were performed to understand the binding interactions of active compounds 14h, 14s and 14t with thrombin protein (PDB ID 1KTS).
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