Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase

Nature

Volumn 521, Issue 7551, 2015, Pages 237-240

  Allegretti, Matteo ^a   Klusch, Niklas ^a   Mills, Deryck J ^a   Vonck, Janet ^a   Kühlbrandt, Werner ^a   Davies, Karen M ^a  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; DIMER; GLUTAMIC ACID; HISTIDINE; PROTON; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SOLVENT; ADENOSINE TRIPHOSPHATE; LIPID BILAYER; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; WATER;

CATALYSIS; ENERGY EFFICIENCY; ENZYME ACTIVITY; MATRIX; MEMBRANE; MITOCHONDRION; PROTEIN; TRANSLOCATION;

ALPHA CHAIN; ALPHA HELIX; ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYOELECTRON MICROSCOPY; HYDROPHILICITY; MEMBRANE; MITOCHONDRIAL MEMBRANE; MITOCHONDRION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTON TRANSPORT; BIOSYNTHESIS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GREEN ALGA; ION TRANSPORT; LIPID BILAYER; METABOLISM; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN SUBUNIT; ROTATION; ULTRASTRUCTURE;

ADENOSINE TRIPHOSPHATE; ARGININE; CHLOROPHYTA; CRYOELECTRON MICROSCOPY; GLUTAMIC ACID; HISTIDINE; ION TRANSPORT; LIPID BILAYERS; MODELS, MOLECULAR; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; PROTON-TRANSLOCATING ATPASES; PROTONS; ROTATION; WATER;

EID: 84927628815     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14185     Document Type: Article

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