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Volumn 39, Issue 1, 2007, Pages 99-107
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Chemical modification of mono-cysteine mutants allows a more global look at conformations of the ε subunit of the ATP synthase from Escherichia coli
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Author keywords
subunit; 3 N maleimidyl propionyl biocytin (MPB); ATP synthase; Chemical modification; Conformational change; Cysteine; Mutagenesis
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Indexed keywords
CYSTEINE;
PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;
ALPHA HELIX;
CARBOXY TERMINAL SEQUENCE;
CATALYSIS;
CONFORMATIONAL TRANSITION;
ELECTROPHORESIS;
ENZYME CONFORMATION;
ENZYME PURIFICATION;
ENZYME SUBUNIT;
ESCHERICHIA COLI;
PROTEIN MODIFICATION;
SHORT SURVEY;
ADENOSINE TRIPHOSPHATE;
BACTERIAL PROTON-TRANSLOCATING ATPASES;
CYSTEINE;
ESCHERICHIA COLI PROTEINS;
HYDROLYSIS;
LYSINE;
MALEIMIDES;
MODELS, MOLECULAR;
MUTATION;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN SUBUNITS;
ESCHERICHIA COLI;
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EID: 34249931153
PISSN: 0145479X
EISSN: 15736881
Source Type: Journal
DOI: 10.1007/s10863-006-9066-6 Document Type: Short Survey |
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Times cited : (7)
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References (42)
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