Structural biology. Nature's rotary electromotors.
Junge
Wolfgang
W
Division of Biophysics, University of Osnabrück, 49069 Osnabrück, Germany. junge@uos.de
Nelson
Nathan
N
D000244:Adenosine Diphosphate / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004563:Electrochemistry; D016983:Enterococcus / Q000201:enzymology*; D045182:Fusobacteria / Q000201:enzymology*; D018698:Glutamic Acid / Q000737:chemistry / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D012964:Sodium / Q000378:metabolism; D055672:Static Electricity
D001426:Bacterial Proteins; D020409:Molecular Motor Proteins; D021122:Protein Subunits; D018698:Glutamic Acid; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D012964:Sodium; D000251:Adenosine Triphosphatases; C500333:F-type sodium ATPase, Ilyobacter tartaricus; C500332:V-type sodium ATPase, Enterococcus hirae