Structure of the alpha subunit of F1-ATPase probed by limited proteolysis.
Open Access
- 1 September 1993
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 268 (25) , 19044-19054
- https://doi.org/10.1016/s0021-9258(17)46733-0
Abstract
No abstract availableThis publication has 43 references indexed in Scilit:
- Correct structure prediction?Nature, 1992
- Isolation and characterisation of a functional αβ heterodimer from the ATP synthase of Rhodospirillum rubrumFEBS Letters, 1992
- The α1β1 heterodimer, the unit of ATP synthaseBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1991
- Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the .epsilon. subunit in the Escherichia coli adenosinetriphosphataseBiochemistry, 1991
- Site-directed mutagenesis of stable adenosine triphosphate synthaseBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1988
- Catalytic and noncatalytic nucleotide binding sites of the Escherichia coli F1 ATPase Amino acid sequences of β‐subunit tryptic peptides labeled with 2‐azido‐ATPFEBS Letters, 1987
- Catalytic and noncatalytic nucleotide binding sites of chloroplast F1 ATPase Photoaffinity labeling and peptide sequencingFEBS Letters, 1987
- Invitro mutated β subunits from the F1-ATPase of the thermophilic bacterium, PS3, containing glutamine in place of glutamic acid in positions 190 or 201 assembles with the α and γ subunits to produce inactive complexesBiochemical and Biophysical Research Communications, 1987
- Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondriaJournal of Molecular Biology, 1985
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970