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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2002-7-31
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pubmed:abstractText |
The yeast Saccharomyces cerevisiae F1F0-ATPase epsilon-subunit (61 residues) was synthesized by the solid-phase peptide approach under both acidic and basic strategies. Only the latter strategy allowed us to obtain a pure epsilon-subunit. The strong propensity of the protein to produce few soluble dimeric species depending on pH has been proved by size-exclusion chromatography, electrophoresis and mass spectrometry. A circular dichroism study showed that an aqueous solution containing 30% trifluoroethanol or 200 mM sodium dodecyl sulphate is required for helical folding. In both solvents at acidic pH, the epsilon-subunit is soluble and monomeric.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1075-2617
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
365-72
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pubmed:dateRevised |
2009-7-10
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pubmed:meshHeading |
pubmed-meshheading:12148785-Amino Acid Sequence,
pubmed-meshheading:12148785-Chromatography, Gel,
pubmed-meshheading:12148785-Chromatography, High Pressure Liquid,
pubmed-meshheading:12148785-Circular Dichroism,
pubmed-meshheading:12148785-Crystallography, X-Ray,
pubmed-meshheading:12148785-Dimerization,
pubmed-meshheading:12148785-Mitochondrial Proton-Translocating ATPases,
pubmed-meshheading:12148785-Molecular Sequence Data,
pubmed-meshheading:12148785-Protein Structure, Secondary,
pubmed-meshheading:12148785-Protein Subunits,
pubmed-meshheading:12148785-Saccharomyces cerevisiae,
pubmed-meshheading:12148785-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12148785-Sequence Alignment,
pubmed-meshheading:12148785-Sequence Homology,
pubmed-meshheading:12148785-Solubility
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pubmed:year |
2002
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pubmed:articleTitle |
Study of the yeast Saccharomyces cerevisiae F1F0-ATPase epsilon-subunit.
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pubmed:affiliation |
Unité de Biophysique Structurale, UMR 5471 CNRS, Université Bordeaux 1, Talence, France.
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pubmed:publicationType |
Journal Article
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