Subunit b-dimer of the Escherichia coli ATP synthase can form left-handed coiled-coils.
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Solution Structure, Determined by Nuclear Magnetic Resonance, of the b30-82 Domain of Subunit b of Escherichia coli F1Fo ATP SynthaseAccommodating discontinuities in dimeric left-handed coiled coils in ATP synthase external stalksThe b subunits in the peripheral stalk of F1F0 ATP synthase preferentially adopt an offset relationshipDomain architecture of the stator complex of the A1A0-ATP synthase from Thermoplasma acidophilum.
P2860
Subunit b-dimer of the Escherichia coli ATP synthase can form left-handed coiled-coils.
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Subunit b-dimer of the Escherichia coli ATP synthase can form left-handed coiled-coils.
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Subunit b-dimer of the Escherichia coli ATP synthase can form left-handed coiled-coils.
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label
Subunit b-dimer of the Escherichia coli ATP synthase can form left-handed coiled-coils.
@ast
Subunit b-dimer of the Escherichia coli ATP synthase can form left-handed coiled-coils.
@en
prefLabel
Subunit b-dimer of the Escherichia coli ATP synthase can form left-handed coiled-coils.
@ast
Subunit b-dimer of the Escherichia coli ATP synthase can form left-handed coiled-coils.
@en
P2860
P1433
P1476
Subunit b-dimer of the Escherichia coli ATP synthase can form left-handed coiled-coils.
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P2093
John G Wise
Pia D Vogel
P2860
P304
P356
10.1529/BIOPHYSJ.107.121012
P407
P577
2008-03-07T00:00:00Z