Correlations of structure and function in subunit c of Escherichia coli F0F1 ATP synthase.
Fillingame
R H
RH
Department of Biomolecular Chemistry, University of Wisconsin Medical School, Madison 53706, USA.
Girvin
M E
ME
Zhang
Y
Y
D000255:Adenosine Triphosphate / Q000096:biosynthesis; D001665:Binding Sites / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D006863:Hydrogen-Ion Concentration; D017136:Ion Transport; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D015394:Molecular Structure; D017354:Point Mutation; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011522:Protons
D011522:Protons; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases