On December 15, 2019, Sahu, Satya Narayan; Pattanayak, Subrat Kumar published an article.Product Details of 456-12-2 The title of the article was Molecular docking and molecular dynamics simulation studies on PLCE1 encoded protein. And the article contained the following:
Phospholipase C epsilon gene (PLCE1) is encoded the 1-phosphatidylinositol 4,5- bisphosphate phosphodiesterase 蔚-1 protein. This protein is characterized by the fetal onset of enormous proteinuria following by severe steroid resistance nephrotic syndrome (SRNS). The mutation position is located on the PIPLC_X domain of PLCE1 encoded protein. Mol. docking study was carried out between aegeline, berberine, diterpenoid, roseoside phytochems. with wild type and mutant of the PIPLC_X domain of the PLCE1 gene encoded protein. From the mol. docking study, it was found that, due to mutation the binding energy was decreased for aegeline, berberine diterpenoid and roseoside with mutant PLCE1 at S1484L compared to wildtype. To achieve the depth anal., we extended our study by performing the mol. dynamic simulation of 100 ns on wild type and the mutant (S1484L) model of above said domain of the studied protein. In the MD simulation study, we analyzed the result obtained from root mean square deviation, root mean square fluctuation, radius of gyration, solvation accessible surface area, hydrogen bond number and principal component anal. These dynamical behavior results of wild type protein show similar behavior with mutant protein. The experimental process involved the reaction of N-(2-Hydroxy-2-(4-methoxyphenyl)ethyl)cinnamamide(cas: 456-12-2).Product Details of 456-12-2
The Article related to mol docking dynamic simulation plce1 phospholipase c epsilon, Enzymes: Structure-Conformation-Active Site and other aspects.Product Details of 456-12-2
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