Article
Characterization of the first cytoplasmic loop of subunit a of the Escherichia coli ATP synthase by surface labeling, cross-linking, and mutagenesis.
The Journal of biological chemistry - 26 Jul 2002
Long Julie C, DeLeon-Rangel Jessica, Vik Steven B
Abstract excerpt
The first cytoplasmic loop of subunit a of the Escherichia coli ATP synthase has been analyzed by cysteine substitution mutagenesis. 13 of the 26 residues tested were found to be accessible to the reaction with 3-(N-maleimidylpropionyl)-biocytin. The other 13 residues predominantly found in the central region of the polypeptide chain between the two transmembrane spans were more resistant to labeling by...
Topics
- Adenosine Triphosphate
- Alanine
- Amino Acid Sequence
- Bacterial Proton-Translocating ATPases
- Cross-Linking Reagents
- Cysteine
- Cytoplasm
- Escherichia coli
- Glutamine
- Immunoblotting
- Leucine
- Molecular Sequence Data
- Mutagenesis, Site-Directed