Distances between active site probes in glutamine synthetase from Escherichia coli: fluorescence energy transfer in free and in stacked dodecamers

Biochemistry ◽  
1986 ◽  
Vol 25 (1) ◽  
pp. 141-151 ◽  
Author(s):  
Michael R. Maurizi ◽  
Philip G. Kasprzyk ◽  
Ann Ginsburg
Keyword(s):  
Escherichia Coli ◽  
Energy Transfer ◽  
Glutamine Synthetase ◽  
Active Site ◽  
Fluorescence Energy Transfer ◽  
Fluorescence Energy

Fluorescence energy transfer experiments with Escherichia coli carbamoyl-phosphate synthetase

Biochemistry ◽  
1983 ◽  
Vol 22 (8) ◽  
pp. 1877-1882 ◽  
Author(s):  
Philip G. Kasprzyk ◽  
Paul M. Anderson ◽  
Joseph J. Villafranca
Keyword(s):  
Escherichia Coli ◽  
Energy Transfer ◽  
Fluorescence Energy Transfer ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Fluorescence Energy

scholarly journals Intramolecular distances between tryptophan residues and the active-site serine residue in alkaline bacterial proteinases as measured by fluorescence energy-transfer studies

1983 ◽  
Vol 215 (2) ◽  
pp. 413-416 ◽  
Author(s):  
N C Genov ◽  
M Shopova ◽  
R Boteva ◽  
F Ricchelli ◽  
G Jori
Keyword(s):  
Energy Transfer ◽  
Active Site ◽  
Three Dimensional ◽  
The Other ◽  
Fluorescence Energy Transfer ◽  
Serine Residue ◽  
Tryptophan Residues ◽  
The One ◽  
Fluorescence Energy

Singlet-singlet energy transfer from the tryptophan residues to an active-site-serine-bound 5-dimethylaminonaphthalene-1-sulphonyl group was investigated in four subtilisins. The transfer distances for subtilisin Novo and mesentericopeptidase are 1.93 +/- 0.20 nm (19.3 +/- 2.0 A) and 1.81 +/- 0.20 nm (18.1 +/- 2.0 A) respectively. The positions of the indole groups in the three-dimensional structures of the two pairs of proteinases, namely subtilisin Novo and mesentericopeptidase on the one hand and subtilisins Carlsberg and DY on the other, are essentially identical.

scholarly journals Fluorescence energy transfer studies on the active site of papain

1980 ◽  
Vol 77 (2) ◽  
pp. 940-943 ◽  
Author(s):  
J. B. Henes ◽  
M. S. Briggs ◽  
S. G. Sligar ◽  
J. S. Fruton
Keyword(s):  
Energy Transfer ◽  
Active Site ◽  
Fluorescence Energy Transfer ◽  
Fluorescence Energy

Fluorescence energy transfer between heterologous active sites of affinity-labeled aspartokinase of Escherichia coli

Biochemistry ◽  
1977 ◽  
Vol 16 (8) ◽  
pp. 1548-1554 ◽  
Author(s):  
Keith Wright ◽  
Mark Takahashi
Keyword(s):  
Escherichia Coli ◽  
Energy Transfer ◽  
Active Sites ◽  
Fluorescence Energy Transfer ◽  
Fluorescence Energy
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