A more robust version of the Arginine 210-switched mutant in subunit a of the Escherichia coli ATP synthase.
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Structure and mechanism of the ATP synthase membrane motor inferred from quantitative integrative modeling.Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linkingOn the question of hydronium binding to ATP-synthase membrane rotorsEssential arginine residue of the F(o)-a subunit in F(o)F(1)-ATP synthase has a role to prevent the proton shortcut without c-ring rotation in the F(o) proton channel.Analysis of an N-terminal deletion in subunit a of the Escherichia coli ATP synthase.
P2860
A more robust version of the Arginine 210-switched mutant in subunit a of the Escherichia coli ATP synthase.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 09 April 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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A more robust version of the A ...... Escherichia coli ATP synthase.
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A more robust version of the A ...... Escherichia coli ATP synthase.
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label
A more robust version of the A ...... Escherichia coli ATP synthase.
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A more robust version of the A ...... Escherichia coli ATP synthase.
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prefLabel
A more robust version of the A ...... Escherichia coli ATP synthase.
@en
A more robust version of the A ...... Escherichia coli ATP synthase.
@nl
P2860
P1476
A more robust version of the A ...... Escherichia coli ATP synthase
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P2093
P2860
P304
P356
10.1016/J.BBABIO.2009.03.022
P407
P50
P577
2009-04-09T00:00:00Z