Comparing the Thermodynamic Stabilities of a Related Thermophilic and Mesophilic Enzyme-Reference-Cited by-同舟云学术

Comparing the Thermodynamic Stabilities of a Related Thermophilic and Mesophilic Enzyme

Published:1999-02-01 Issue:8 Volume:38 Page:2570-2576
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Beadle Beth M.¹,Baase Walter A.¹,Wilson David B.¹,Gilkes Neil R.¹,Shoichet Brian K.¹

Affiliation:

1. Department of Molecular Pharmacology & Biological Chemistry, Northwestern University, 303 East Chicago Avenue, Chicago, Illinois 60611-3008, Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403, Section of Biochemistry, Molecular & Cell Biology, Cornell University, Ithaca, New York 14853, and Department of Microbiology, University of British Columbia, Vancouver, Canada

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9824902

Reference34 articles.

1. Crystal structure of thermitase at 1.4A˚resolution

2. Reversible thermal unfolding of thermostable phosphoglycerate kinase. Thermostability associated with mean zero enthalpy change

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