Effect of single amino acid replacements on the folding and stability of dihydrofolate reductase from Escherichia coli-Reference-Cited by-同舟云学术

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Effect of single amino acid replacements on the folding and stability of dihydrofolate reductase from Escherichia coli

Published:1987-05-19 Issue:10 Volume:26 Page:2674-2682
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Perry Kathleen M.,Onuffer James J.,Touchette Nancy A.,Herndon Cinda S.,Gittelman Mitchell S.,Matthews Robert C.,Chen Jin Tan,Mayer Ruth J.,Taira Kazunari

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00384a004

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1. Mutational analysis confirms the presence of distal inhibitor-selectivity determining residues in B. stearothermophilus dihydrofolate reductase;Archives of Biochemistry and Biophysics;2020-10

2. Halophilic mechanism of the enzymatic function of a moderately halophilic dihydrofolate reductase from Haloarcula japonica strain TR-1;Extremophiles;2017-03-27

3. Quality Matters: Extension of Clusters of Residues with Good Hydrophobic Contacts Stabilize (Hyper)Thermophilic Proteins;Journal of Chemical Information and Modeling;2014-01-28

4. Autotransporters: The Cellular Environment Reshapes a Folding Mechanism to Promote Protein Transport;The Journal of Physical Chemistry Letters;2012-04-10

5. ATP-Independent Control of Autotransporter Virulence Protein Transport via the Folding Properties of the Secreted Protein;Chemistry & Biology;2012-02

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