De novo sequence redesign of a functional Ras‐binding domain globally inverted the surface charge distribution and led to extreme thermostability-Reference-Cited by-同舟云学术

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De novo sequence redesign of a functional Ras‐binding domain globally inverted the surface charge distribution and led to extreme thermostability

Published:2021-03 Issue:5 Volume:118 Page:2031-2042
ISSN:0006-3592
Container-title:Biotechnology and Bioengineering
language:en
Short-container-title:Biotech & Bioengineering

Author:

Liu Ruicun¹^ORCID,Wang Jichao¹,Xiong Peng¹,Chen Quan¹²,Liu Haiyan¹²³

Affiliation:

1. School of Life Sciences University of Science and Technology of China Hefei Anhui China

2. Hefei National Laboratory for Physical Sciences at the Microscale University of Science and Technology of China Hefei Anhui China

3. School of Data Science University of Science and Technology of China Hefei Anhui China

Publisher

Wiley

Subject

Applied Microbiology and Biotechnology,Bioengineering,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/bit.27716

Reference48 articles.

1. Approaching boiling point stability of an alcohol dehydrogenase through computationally‐guided enzyme engineering;Aalbers F. S.;eLife,2020

2. Mutational effects on stability are largely conserved during protein evolution

3. What has de novo protein design taught us about protein folding and biophysics?

4. Bellman R. D. Holgate M. A. &Sugar T. G.(2008).SPARKy 3: Design of an active robotic ankle prosthesis with two actuated degrees of freedom using regenerative kinetics. Paper presented at the 2008 2nd IEEE RAS & EMBS International Conference on Biomedical Robotics and Biomechatronics 511–516.

5. Automated selection of stabilizing mutations in designed and natural proteins

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