A barrel in the stalk
- 1 November 1995
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 2 (11), 915-918
- https://doi.org/10.1038/nsb1195-915
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopyNature Structural & Molecular Biology, 1995
- The γ subunit in the Escherichia coli ATP synthase complex (ECF1F0) extends through the stalk and contacts the c subunits of the F0 partFEBS Letters, 1995
- Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondriaNature, 1994
- Hairpin folding of subunit c of F1Fo ATP synthase: 1H distance measurements to nitroxide-derivatized aspartyl-61Biochemistry, 1994
- The atp2 operon of the green bacterium Chlorobium limicolaBiochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1993
- In Situ Regulation of Chloroplast Coupling Factor ActivityAnnual Review of Plant Physiology and Plant Molecular Biology, 1992
- Nucleotide-dependent and dicyclohexylcarbodiimide-sensitive conformational changes in the .epsilon. subunit of Escherichia coli ATP synthaseBiochemistry, 1991
- The mitochondrial ATP synthase inhibitor protein binds near the C‐terminus of the F1 β‐subunitFEBS Letters, 1988
- E. coli F1-ATPase interacts with a membrane protein component of a proton channelNature, 1982
- Characterization of the inhibitory (.epsilon.) subunit of the proton-translocating adenosine triphosphatase from Escherichia coliBiochemistry, 1980