pubmed-article:12148785 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12148785 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
pubmed-article:12148785 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:12148785 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
pubmed-article:12148785 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:12148785 | pubmed:dateCreated | 2002-7-31 | lld:pubmed |
pubmed-article:12148785 | 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. | lld:pubmed |
pubmed-article:12148785 | pubmed:language | eng | lld:pubmed |
pubmed-article:12148785 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12148785 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12148785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12148785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12148785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12148785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12148785 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12148785 | pubmed:month | Jul | lld:pubmed |
pubmed-article:12148785 | pubmed:issn | 1075-2617 | lld:pubmed |
pubmed-article:12148785 | pubmed:author | pubmed-author:Aznar-Derunes... | lld:pubmed |
pubmed-article:12148785 | pubmed:author | pubmed-author:ManigandClaud... | lld:pubmed |
pubmed-article:12148785 | pubmed:author | pubmed-author:PicardPhilipp... | lld:pubmed |
pubmed-article:12148785 | pubmed:author | pubmed-author:DautantAlainA | lld:pubmed |
pubmed-article:12148785 | pubmed:author | pubmed-author:GoetzMichaelM | lld:pubmed |
pubmed-article:12148785 | pubmed:author | pubmed-author:SchmitterJean... | lld:pubmed |
pubmed-article:12148785 | pubmed:author | pubmed-author:PrecigouxGill... | lld:pubmed |
pubmed-article:12148785 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12148785 | pubmed:volume | 8 | lld:pubmed |
pubmed-article:12148785 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12148785 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12148785 | pubmed:pagination | 365-72 | lld:pubmed |
pubmed-article:12148785 | pubmed:dateRevised | 2009-7-10 | lld:pubmed |
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pubmed-article:12148785 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12148785 | pubmed:articleTitle | Study of the yeast Saccharomyces cerevisiae F1F0-ATPase epsilon-subunit. | lld:pubmed |
pubmed-article:12148785 | pubmed:affiliation | Unité de Biophysique Structurale, UMR 5471 CNRS, Université Bordeaux 1, Talence, France. | lld:pubmed |
pubmed-article:12148785 | pubmed:publicationType | Journal Article | lld:pubmed |