Dissecting the Effect of Temperature on Hyperthermophilic Pf2001 Esterase Dimerization by Molecular Dynamics
Author:
Affiliation:
1. Institute of Theoretical Chemistry, College of Chemistry, Jilin University, Changchun 130023, China
2. School of Pharmaceutical Sciences, Jilin University, Changchun 130021, China
Funder
Jilin University
Publisher
American Chemical Society (ACS)
Subject
Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jcim.3c00415
Reference48 articles.
1. Overview of strategies for developing high thermostability industrial enzymes: Discovery, mechanism, modification and challenges
2. Biotechnological applications of archaeal enzymes from extreme environments
3. The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus 1 1Edited by R. Huber
4. Functional and structural features of the oxyanion hole in a thermophilic esterase from Alicyclobacillus acidocaldarius
5. Crystal Structure and Biochemical Properties of a Novel Thermostable Esterase Containing an Immunoglobulin-Like Domain
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