Article
Conformational changes of the H+-ATPase from Escherichia coli upon nucleotide binding detected by single molecule fluorescence.
FEBS letters - 23 Oct 1998
Börsch M, Turina P, Eggeling C, Fries J R, Seidel C A, Labahn A, Gräber P
Abstract excerpt
Using a confocal fluorescence microscope with an avalanche photodiode as detector, we studied the fluorescence of the tetramethylrhodamine labeled F1 part of the H+-ATPase from Escherichia coli, EF1, carrying the gammaT106-C mutation [Aggeler, J.A. and Capaldi, R.A. (1992) J. Biol. Chem. 267, 213...
Topics
- Amino Acid Substitution
- Escherichia coli
- Mutation
- Nucleotides
- Protein Binding
- Protein Conformation
- Proton-Translocating ATPases
- Spectrometry, Fluorescence