Structural model of the transmembrane Fo rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ
- 1 October 2002
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Biomembranes
- Vol. 1565 (2) , 232-245
- https://doi.org/10.1016/s0005-2736(02)00572-2
Abstract
No abstract availableKeywords
This publication has 76 references indexed in Scilit:
- F‐ATPase: specific observation of the rotating c subunit oligomer of EFoEF1FEBS Letters, 2000
- Molecular Architecture of the Rotary Motor in ATP SynthaseScience, 1999
- Direct indication for the existence of a double stalk in CF0F1Journal of Molecular Biology, 1998
- Molecular architecture of the c-subunit oligomer in the membrane domain of F-ATPases probed by tryptophan substitution mutagenesisJournal of Molecular Biology, 1998
- Solution Structure of the Transmembrane H+-Transporting Subunit c of the F1Fo ATP SynthaseBiochemistry, 1998
- Apoprotein structure in the LH2 complex from Rhodopseudomonas acidophila strain 10050: modular assembly and protein pigment interactions 1 1Edited by R. HuberJournal of Molecular Biology, 1997
- Topographical structure of membrane‐bound Escherichia coli F1F0 ATP synthase in aqueous bufferFEBS Letters, 1996
- Molecular imaging of Escherichia coli F0F1‐ATPase in reconstituted membranes using atomic force microscopyFEBS Letters, 1996
- Electron-crystallographic Refinement of the Structure of BacteriorhodopsinJournal of Molecular Biology, 1996
- Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopyNature Structural & Molecular Biology, 1995