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. 2008:2008:469062.
doi: 10.1155/2008/469062.

The crystal water affect in the interaction between the tenebrio molitor alpha-amylase and its inhibitor

Zhu Zhi-Fei  1 , Ning Ting-Ting, Xu Zu-Min, Zhang Ge-Xin, Ma Yan-He
Affiliations

The crystal water affect in the interaction between the tenebrio molitor alpha-amylase and its inhibitor

Zhu Zhi-Fei et al. Bioinorg Chem Appl. 2008.

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.

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Figures

Figure 1
Figure 1
The respective chart of ΔE among 3 monomers.
Figure 2
Figure 2
The compositive chart of ΔE in different crystal water proportion.
Figure 3
Figure 3
The respective chart of ΔE in different crystal water proportion.
Figure 4
Figure 4
The chart of ΔE in polarizability crystal water proportion.
See this image and copyright information in PMC

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