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Enzymatic protein switches built from paralogous input domains

Published:2015-10-26 Issue:4 Volume:113 Page:852-858
ISSN:0006-3592
Container-title:Biotechnology and Bioengineering
language:en
Short-container-title:Biotechnol. Bioeng.

Author:

Tullman Jennifer¹,Nicholes Nathan¹,Dumont Matt R.¹,Ribeiro Lucas F.¹,Ostermeier Marc¹

Affiliation:

1. Department of Chemical and Biomolecular EngineeringJohns Hopkins University3400 N. Charles St. Maryland Hall 119BaltimoreMD21218

Funder

National Science Foundation

Defense Threat Reduction Agency

São Paulo Research Foundation

Publisher

Wiley

Subject

Applied Microbiology and Biotechnology,Bioengineering,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/bit.25852

Reference30 articles.

1. Purification and properties of a periplasmic D-xylose-binding protein from Escherichia coli K-12.

2. Structure of the Escherichia coli Phosphonate Binding Protein PhnD and Rationally Optimized Phosphonate Biosensors

3. Non-allosteric enzyme switches possess larger effector-induced changes in thermodynamic stability than their non-switch analogs

4. Design of protein switches based on an ensemble model of allostery

5. Rational design of a ligand-controlled protein conformational switch

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3. In vivo protein-based biosensors: seeing metabolism in real time;Trends in Biotechnology;2023-01

4. Chimeric Protein Switch Biosensors;Advances in Biochemical Engineering/Biotechnology;2023

5. Exploring Performance Parameters of Artificial Allosteric Protein Switches;Journal of Molecular Biology;2022-09

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