Time-resolved fluorescence studies of tryptophan mutants ofEscherichia coliglutamine synthetase: Conformational analysis of intermediates and transition-state complexes
Author:
Funder
National Institutes of Health and UIUC
NIH
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560010306/fullpdf
Reference40 articles.
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2. Interpretation of fluorescence decays in proteins using continuous lifetime distributions;Alcala;Biophys. J.,1987
3. Novel subunit-subunit interactions in Escherichia coli glutamine synthetase;Almassy;Nature,1986
4. Time-resolved fluorescence studies of genetically engineered E. coli glutamine synthetase: Effects of ATP on the Trp-57 loop;Atkins;Biochemistry,1991
5. Physical and genetic characterization of the glnA-glnG region of the Escherichia coli chromosome;Backman;Proc. Natl. Acad. Sci. USA,1981
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1. The central loop of Escherichia coli glutamine synthetase is flexible and functionally passive;Archives of Biochemistry and Biophysics;2005-04
2. Site-directed mutagenesis of Cys-92 from the α-polypeptide of Phaseolus vulgaris glutamine synthetase reveals that this highly conserved residue is not essential for enzyme activity but it is involved in thermal stability;Plant Science;2000-05
3. Functional importance of Asp56 from the alpha-polypeptide of Phaseolus vulgaris glutamine synthetase . An essential residue for transferase but not for biosynthetic enzyme activity;European Journal of Biochemistry;1999-09
4. Investigating the effects of posttranslational adenylylation on the metal binding sites ofEscherichia coliglutamine synthetase using lanthanide luminescence spectroscopy;Protein Science;1996-12
5. The effect of groES on the groEL-dependent assembly of dodecameric glutamine synthetase in the presence of ATP and ADP.;Journal of Biological Chemistry;1994-05
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