An efficient method to predict protein thermostability in alanine mutation

Author:

Gao Ya1ORCID,Wang Bo2,Hu Shiyu3,Zhu Tong23ORCID,Zhang John Z. H.234

Affiliation:

1. School of Mathematics, Physics and Statistics, Shanghai University of Engineering Science, Shanghai 201620, China

2. Shanghai Engineering Research Center of Molecular Therapeutics & New Drug Development, School of Chemistry and Molecular Engineering, East China Normal University, Shanghai 200062, China

3. NYU-ECNU Center for Computational Chemistry at NYU Shanghai, Shanghai 200062, China

4. Shenzhen Institute of Synthetic Biology, Faculty of Synthetic Biology, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China

Abstract

An efficient method to predict protein thermostability in alanine mutation was proposed.

Funder

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Reference76 articles.

1. Computational design of protein–protein interactions

2. Progress in computational protein design

3. G. L.Butterfoss and B.Kuhlman , Computer-based design of novel protein structures , Annual Review of Biophysics and Biomolecular Structure , 2006 , vol. 35, pp. 49–65

4. Design of a Novel Globular Protein Fold with Atomic-Level Accuracy

5. Principles that Govern the Folding of Protein Chains

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