ATP causes a large change in the conformation of the isolated alpha subunit of Escherichia coli F1 ATPase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
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1. Energetic Effects of Magnesium in the Recognition of Adenosine Nucleotides by the F1-ATPase β Subunit;Biochemistry;2010-06-02
2. Nucleotide Binding Drives Conformational Changes in the Isolated α and β Subunits of the F1-ATPase from Escherichia coli;Biochemical and Biophysical Research Communications;1999-12
3. Modification of domains of α and β subunits of F1-ATPase from the thermophylic bacterium PS3, in their isolated and associated forms, by 3′-O-(4-benzoyl)benzoyl adenosine 5′-triphosphate (BzATP);Journal of Bioenergetics and Biomembranes;1996-12
4. Our primary source of ATP;Nature;1994-08
5. Combined application of site-directed mutagenesis, 2-azido-ATP labeling, and lin-benzo-ATP binding to study the noncatalytic sites of Escherichia coli F1-ATPase.;Journal of Biological Chemistry;1993-03
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