Resolution of the fluorescence of the buried tryptophan in yeast 3-phosphoglycerate kinase using succinimide
- 8 March 1991
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1077 (1) , 19-24
- https://doi.org/10.1016/0167-4838(91)90520-a
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Assignment of the heterogeneous static and time-resolved tryptophan fluorescence of 3-phosphoglycerate kinaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989
- Detection of intermediates in the unfolding transition of phosphoglycerate kinase using limited proteolysisBiochemistry, 1989
- Frequency domain fluorescence studies of yeast phosphoglycerate kinase and its ternary complexEuropean Journal of Biochemistry, 1987
- The resolution of heterogeneous fluorescence of multitryptophan‐containing proteins studied by a fluorescence‐quenching methodEuropean Journal of Biochemistry, 1986
- The folding and mutual interaction of the domains of yeast 3‐phosphoglycerate kinaseEuropean Journal of Biochemistry, 1985
- Biochemistry: Dynamic proteinsNature, 1983
- Fluorescence quenching of liver alcohol dehydrogenase by acrylamideBiochemistry, 1982
- Fluorescence quenching studies with proteinsAnalytical Biochemistry, 1981
- Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzymeNature, 1979
- Nuclear‐Magnetic‐Resonance Study of the Active‐Site Structure of Yeast Phosphoglycerate KinaseEuropean Journal of Biochemistry, 1976