Quantifying Protein Electrostatic Interactions in Cells by Nuclear Magnetic Resonance Spectroscopy-Reference-Cited by-同舟云学术

Quantifying Protein Electrostatic Interactions in Cells by Nuclear Magnetic Resonance Spectroscopy

Published:2021-11-12 Issue:46 Volume:143 Page:19606-19613
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Song Xiangfei¹²,Wang Mengting¹²³,Chen Xiaoxu¹²³,Zhang Xueying¹²³,Yang Ying¹²,Liu Zhijun⁴,Yao Lishan¹²^ORCID

Affiliation:

1. Qingdao New Energy Shandong Laboratory, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, China

2. Shandong Energy Institute, Qingdao 266101, China

3. University of Chinese Academy of Sciences, Beijing 100049, China

4. National Facility for Protein Science, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201210, China

Funder

Shandong Provincial Natural Science Foundation

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.1c10154

Reference50 articles.

1. Rational stabilization of enzymes by computational redesign of surface charge–charge interactions

2. Modulation of folding energy landscape by charge–charge interactions: Linking experiments with computational modeling

3. Alterations of Nonconserved Residues Affect Protein Stability and Folding Dynamics through Charge–Charge Interactions

4. A Detailed Thermodynamic Analysis of Ras/Effector Complex Interfaces

5. The role of DNA shape in protein–DNA recognition

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