Conformational changes of the H+-ATPase from Escherichia coli upon nucleotide binding detected by single molecule fluorescence.
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, 21355-...
المؤلفون الرئيسيون: | Börsch, M, Turina, P, Eggeling, C, Fries, JR, Seidel, C, Labahn, A, Gräber, P |
---|---|
التنسيق: | Journal article |
اللغة: | English |
منشور في: |
1998
|
مواد مشابهة
-
Monitoring conformational dynamics of a single molecule by selective fluorescence spectroscopy.
حسب: Eggeling, C, وآخرون
منشور في: (1998) -
The ATPase Activity of Escherichia coli Expressed AAA+-ATPase Protein
حسب: Amita Kaundal, وآخرون
منشور في: (2020-08-01) -
Quantitative identification of different single molecules by selective time-resolved confocal fluorescence spectroscopy
حسب: Fries, JR, وآخرون
منشور في: (1998) -
High-resolution single-molecule characterization of the enzymatic states in Escherichia coli F1-ATPase.
حسب: Bilyard, T, وآخرون
منشور في: (2013) -
High-resolution single-molecule characterization of the enzymatic states in Escherichia coli F1-ATPase
حسب: Bilyard, T, وآخرون
منشور في: (2013)