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The amino acid residues (Met1, Asp2, Glu43, Ala44, Glu47, Lys51, Ala157 and Leu158) lining in the binding site were predicted using SiteMap.
On an average, atleast two residues per binding site were predicted to have ∆∆G score ≥ 0.5.
The substituted benzene moieties of 6 and 7, which were oriented towards the opposite site of the mPGES-1 binding site, were predicted to be embedded in a hydrophobic site formed by mainly aromatic or hydrophobic amino acids (e.g., Tyr28, Tyr130, Thr131, Ala31, and Ile32).
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The CRLI carbohydrate binding site was predicted by docking with a specific inhibitory trisaccharide.
The TF binding site was predicted using an online database RegPrecise (http://regprecise.lbl.gov/RegPrecise/index.jsp) and Target Explorer (http://te.cryst.bbk.ac.uk/).ac.uk/
Furthermore, a DNA binding site was predicted in this protein model.
The substrate binding site was predicted by using the CastP server [34].
However a binding site was predicted by the RNA22 algorithm which does not rely on cross-species conservation of binding sites for prediction.
An edge f→g is added to the graph only when at least one binding site is predicted around the target gene, so when sf,g≥1.
The nonlocal nature of the protein-ligand binding problem is investigated via the Gaussian Network Model with which the residues lying along interaction pathways in a protein and the residues at the binding site are predicted.
Important amino acid involved in ligand binding site is predicted by this server.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com