Conformational changes in yeast phosphoglycerate kinase upon ligand binding: Fluorescence of a linked probe and chemical reactivity of genetically introduced cysteinyl residues-Reference-Cited by-同舟云学术

Conformational changes in yeast phosphoglycerate kinase upon ligand binding: Fluorescence of a linked probe and chemical reactivity of genetically introduced cysteinyl residues

Published:1991-04 Issue:4 Volume:10 Page:315-324
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Genetics
language:en
Short-container-title:Proteins

Author:

Desmadril Michel,Minard Philippe,Ballery Nathalie,Gaillard-Miran Sophie,Hall Len,Yon Jeannine M.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference34 articles.

1. Purification of 3-phosphoglycerate kinase from diverse sources by affinity elution chromatography

2. Phosphoglycerate kinase In: “The Enzymes,” vol. 8, 3rd ed, (ed.). New York: Academic Press, 1973: 335-351

3. Structure of Yeast Phosphoglycerate Kinase

4. Sequence and structure of yeast phosphoglycerate kinase.

5. Structure of horse muscle phosphoglycerate kinase

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2. Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase;FEBS Journal;2005-03-29

3. Structure of a circularly permuted phosphoglycerate kinase;Acta Crystallographica Section D Biological Crystallography;2002-11-26

4. Conformational dynamics and enzyme activity;Biochimie;1998-01

5. Substrate-induced conformational changes in yeast 3-phosphoglycerate kinase monitored by fluorescence of single tryptophan probes;Protein Science;1996-06