Comparative molecular dynamics simulations identify a salt-sensitive loop responsible for the halotolerant activity of GH5 cellulases
Author:
Affiliation:
1. Taishan College, Shandong University, Qingdao, China
2. State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China
3. National Glycoengineering Research Center, Shandong University, Qingdao, China
Funder
National Key Research and Development Project
National Natural Science Foundation of China
Key Research and Development Project of Shandong Province
Publisher
Informa UK Limited
Subject
Molecular Biology,General Medicine,Structural Biology
Link
https://www.tandfonline.com/doi/pdf/10.1080/07391102.2021.1930167
Reference43 articles.
1. Structural Insights from Molecular Dynamics Simulations of Tryptophan 7-Halogenase and Tryptophan 5-Halogenase
2. Molecular dynamics of the salt dependence of a cold-adapted enzyme: endonuclease I
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4. Improved biocatalysts by directed evolution and rational protein design
5. Engineering the third wave of biocatalysis
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