Selection and analyses of variants of a designed protein suggest importance of hydrophobicity of partially buried sidechains for protein stability at high temperatures-Reference-Cited by-同舟云学术

Selection and analyses of variants of a designed protein suggest importance of hydrophobicity of partially buried sidechains for protein stability at high temperatures

Published:2019-05-23 Issue:8 Volume:28 Page:1437-1447
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Han Mingjie¹,Liao Sanhui¹,Peng Xiong¹,Zhou Xiaoqun¹,Chen Quan¹^ORCID,Liu Haiyan¹²³

Affiliation:

1. School of Life SciencesUniversity of Science and Technology of China Hefei Anhui China

2. School of Data ScienceUniversity of Science and Technology of China Hefei Anhui China

3. Hefei National Laboratory for Physical Sciences at the Microscale Hefei Anhui China

Funder

National Natural Science Foundation of China

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.3643

Reference34 articles.

1. Electrostatic Contribution of Surface Charge Residues to the Stability of a Thermophilic Protein: Benchmarking Experimental and Predicted pKa Values

2. Hydrophobic Effect on the Stability and Folding of a Hyperthermophilic Protein

3. Contribution of hydrophobic interactions to protein stability

4. Protein Thermal Stability Enhancement by Designing Salt Bridges: A Combined Computational and Experimental Study

5. Contribution of hydrogen bonds to protein stability

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