title: The crystal water affect in the interaction between the tenebrio molitor alpha-amylase and its inhibitor.
abstract: Molecular dynamics simulation of the interaction between the Tenebrio molitor alpha-amylase and its inhibitor at different proportion of crystal water was carried out with OPLS force field by hyperchem 7.5 software. In the correlative study, the optimal temperature of wheat monomeric and dimeric protein inhibitors was from 273 K to 318 K. The the average temperature of experimentation is 289 K. (1) The optimal temperature of interaction between alpha-amylase and its inhibitors was 280 K without crystal water that was close to the results of experimentation. The forming of enzyme-water and inhibitor-water was easy, but incorporating third monomer was impossible. (2) Having analyzed the potential energy data, the optimal temperature of interaction energy between alpha-amylase and its inhibitors covering 9 : 1, 5 : 5, 4 : 6, and 1 : 9 proportion crystal water was 290 K. (3) We compared the correlative QSAR properties. The proportion of crystal water was close to the data of polarizability (12.4%) in the QSAR properties. The optimal temperature was 280 K. This result was close to 289 K. These findings have theoretical and practical implications.
authors.affiliation: School of Chemical and Material Engineering, Jiangnan University, Wuxi, Jiangsu 214122, China.
authors.forename: Zhu
authors.initials: Z
authors.lastname: Zhi-Fei
authors.forename: Ning
authors.initials: N
authors.lastname: Ting-Ting
authors.forename: Xu
authors.initials: X
authors.lastname: Zu-Min
authors.forename: Zhang
authors.initials: Z
authors.lastname: Ge-Xin
authors.forename: Ma
authors.initials: M
authors.lastname: Yan-He