Thermal Unfolding Used As a Probe To Characterize the Intra- and Intersubunit Stabilizing Interactions in Phosphorylating d-Glyceraldehyde-3-phosphate Dehydrogenase from Bacillus stearothermophilus-Reference-Cited by-同舟云学术

Thermal Unfolding Used As a Probe To Characterize the Intra- and Intersubunit Stabilizing Interactions in Phosphorylating d-Glyceraldehyde-3-phosphate Dehydrogenase from Bacillus stearothermophilus

Published:2002-05-18 Issue:24 Volume:41 Page:7556-7564
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Roitel Olivier¹,Ivinova Olga¹,Muronetz Vladimir¹,Nagradova Natalia¹,Branlant Guy¹

Affiliation:

1. Maturation des ARN et Enzymologie Moléculaire, UMR 7567 CNRS-UHP, Université Henri Poincaré Nancy I, BP 239, 54506 Vandoeuvre-lès-Nancy Cedex, France, and A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi012084%2B

Reference26 articles.

1. Use of site-directed mutagenesis to probe the role of Cys149 in the formation of charge-transfer transition in glyceraldehyde-3-phosphate dehydrogenase

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