On May 31, 2010, Yoshida, Tatsusada; Munei, Yohei; Hitaoka, Seiji; Chuman, Hiroshi published an article.Recommanded Product: 3-Nitro-4-chlorobenzenesulfonamide The title of the article was Correlation Analyses on Binding Affinity of Substituted Benzenesulfonamides with Carbonic Anhydrase Using ab Initio MO Calculations on Their Complex Structures. And the article contained the following:
Quant. structure-activity relationship analyses on the free energy change during complex formation between substituted benzenesulfonamides (BSAs) and bovine carbonic anhydrase II (bCA II) were performed using generalized Born/surface area (GB/SA) and ab initio fragment MO (FMO) calculations for the whole complex structures. The result shows that the overall free energy change is governed by the contribution from solvation and dissociation free energy changes accompanying complex formation. The FMO-IFIE (interfragment interaction energy) anal. quant. revealed that the intrinsic interaction energy of bCA II with BSAs is mostly from interactions with amino acid residues in the active site of bCA II. The “Zn block” (Zn2+ and three histidine residues coordinated to Zn2+) in the active site shows the lowest interaction energy and the greatest variance of interaction energy with BSAs through their coordination interaction. The proposed procedure was demonstrated to provide a quant. basis for understanding a ligand-protein interaction at electronic and at. levels. The experimental process involved the reaction of 3-Nitro-4-chlorobenzenesulfonamide(cas: 97-09-6).Recommanded Product: 3-Nitro-4-chlorobenzenesulfonamide
The Article related to binding affinity model benzenesulfonamide derivative carbonic anhydrase, Enzymes: Substrates-Cofactors-Inhibitors-Activators-Coenzymes-Products and other aspects.Recommanded Product: 3-Nitro-4-chlorobenzenesulfonamide
Referemce:
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