(2018) Disulfide bridge formation to increase thermostability of DFPase enzyme: A computational study. Computational Biology and Chemistry. pp. 272-278. ISSN 1476-9271
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Abstract
Organophosphate compounds bioremediation by use of organophosphorus degradation enzymes such as DFPase is a developing interest in industry and medicine. The most important problem with the bio-catalytic enzymes is their instability on high temperatures. This work carried out to find suitable locations for introducing disulfide bridges in DFPase enzyme. We employed some computational approaches to design the disulfide bridges and evaluate their roles in the enzyme structural thermostability. According to the in silico results, mutant 6 (V24C, C76) increased the enzyme thermostability relative to wild-type.
Item Type: | Article |
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Keywords: | DFPase Protein thermostability Disulfide bridge MD simulation diisopropyl fluorophosphatase molecular-dynamics crystal-structure loligo-vulgaris diisopropylfluorophosphatase stability site bond mechanism proteins Life Sciences & Biomedicine - Other Topics Computer Science |
Divisions: | |
Page Range: | pp. 272-278 |
Journal or Publication Title: | Computational Biology and Chemistry |
Journal Index: | ISI |
Volume: | 77 |
Identification Number: | https://doi.org/10.1016/j.compbiolchem.2018.09.005 |
ISSN: | 1476-9271 |
Depositing User: | مهندس مهدی شریفی |
URI: | http://eprints.bmsu.ac.ir/id/eprint/2931 |
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