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Analysis of the thermostability determinants of hyperthermophilic esterase EstE1 based on its predicted three-dimensional structure

Authors
Rhee, JKKim, DYAhn, DGYun, JHJang, SHShin, HCCho, HSPan, JGOh, JW
Issue Date
Apr-2006
Publisher
AMER SOC MICROBIOLOGY
Citation
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, v.72, no.4, pp.3021 - 3025
Journal Title
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Volume
72
Number
4
Start Page
3021
End Page
3025
URI
http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/18646
DOI
10.1128/AEM.72.4.3021-3025.2006
ISSN
0099-2240
Abstract
The three-dimensional (3D) structure of the hyperthermophilic esterase EstE1 was constructed by homology modeling using Archaeoglobus fulgidus esterase as a reference, and the thermostability-structure relationship was analyzed. Our results verified the predicted 3D structure of EstE1 and identified the ion pair networks and hydrophobic interactions that are critical determinants for the thermostability of EstE1.
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