An additional acidic residue in the membrane portion of the b-subunit of the energy-transducing adenosine triphosphatase of Escherichia coli affects both assembly and function.
about
Complementation between uncF alleles affecting assembly of the F1F0-ATPase complex of Escherichia coli.A mutation in which alanine 128 Is replaced by aspartic acid abolishes dimerization of the b-subunit of the F0F1-ATPase from Escherichia coli.Bacterial adenosine 5'-triphosphate synthase (F1F0): purification and reconstitution of F0 complexes and biochemical and functional characterization of their subunits.Proton conduction by subunit a of the membrane-bound ATP synthase of Escherichia coli revealed after induced overproduction.Random mutagenesis of the gene for the beta-subunit of F1-ATPase from Escherichia coli.Insertion scanning mutagenesis of subunit a of the F1F0 ATP synthase near His245 and implications on gating of the proton channel.
P2860
An additional acidic residue in the membrane portion of the b-subunit of the energy-transducing adenosine triphosphatase of Escherichia coli affects both assembly and function.
description
1984 nî lūn-bûn
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1984年の論文
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1984年論文
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1984年論文
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1984年論文
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1984年論文
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1984年論文
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1984年论文
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1984年论文
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1984年论文
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name
An additional acidic residue i ...... ts both assembly and function.
@en
type
label
An additional acidic residue i ...... ts both assembly and function.
@en
prefLabel
An additional acidic residue i ...... ts both assembly and function.
@en
P2093
P2860
P356
P1433
P1476
An additional acidic residue i ...... ts both assembly and function.
@en
P2093
P2860
P356
10.1042/BJ2210043
P407
P577
1984-07-01T00:00:00Z