Charge Engineering Improves the Performance of Bst DNA Polymerase Fusions-Reference-Cited by-同舟云学术

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Charge Engineering Improves the Performance of Bst DNA Polymerase Fusions

Published:2022-03-23 Issue:4 Volume:11 Page:1488-1496
ISSN:2161-5063
Container-title:ACS Synthetic Biology
language:en
Short-container-title:ACS Synth. Biol.

Author:

Paik Inyup¹²^ORCID,Bhadra Sanchita¹²^ORCID,Ellington Andrew D.¹²^ORCID

Affiliation:

1. Department of Molecular Biosciences, College of Natural Sciences, The University of Texas at Austin, Austin, Texas 78712, United States

2. Center for Systems and Synthetic Biology, The University of Texas at Austin, Austin, Texas 78712, United States

Funder

Welch Foundation

Division of Molecular and Cellular Biosciences

National Institute of Biomedical Imaging and Bioengineering

National Aeronautics and Space Administration

Publisher

American Chemical Society (ACS)

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous),Biomedical Engineering,General Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/acssynbio.1c00559

Reference37 articles.

1. Protein Stability and Surface Electrostatics: A Charged Relationship

2. Supercharging Proteins Can Impart Unusual Resilience

3. Surface supercharged human enteropeptidase light chain shows improved solubility and refolding yield

4. Structure-Based Design of Supercharged, Highly Thermoresistant Antibodies

5. Arginine to Lysine Mutations Increase the Aggregation Stability of a Single-Chain Variable Fragment through Unfolded-State Interactions

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5. Double domain fusion improves the reverse transcriptase activity and inhibitor tolerance of Bst DNA polymerase;International Journal of Biological Macromolecules;2024-08

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