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Volumn 426, Issue 1, 1998, Pages 37-40
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Trapping of conformations of the Escherichia coli F1 ATPase by disulfide bond formation: A state of the enzyme with all three catalytic sites of equal and low affinity for nucleotides
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Author keywords
Catalytic site nucleotide binding; F1 Adenosine triosatase, cross linking; Subunit conformation
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Indexed keywords
ADENOSINE TRIPHOSPHATASE;
ADENOSINE TRIPHOSPHATE;
EDETIC ACID;
AMINO ACID SEQUENCE;
ARTICLE;
CONFORMATIONAL TRANSITION;
CROSS LINKING;
DISULFIDE BOND;
ENZYME ACTIVE SITE;
ENZYME BINDING;
ENZYME CONFORMATION;
ENZYME SPECIFICITY;
ENZYME SUBUNIT;
ESCHERICHIA COLI;
MUTATION;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN PROTEIN INTERACTION;
ESCHERICHIA COLI;
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EID: 0032503036
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/S0014-5793(98)00306-8 Document Type: Article |
Times cited : (5)
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References (30)
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