Study of the yeast Saccharomyces cerevisiae F1F0-ATPase epsilon-subunit. |
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Authors: | Céline Aznar-Derunes Claude Manigand Philippe Picard Alain Dautant Michael Goetz Jean-Marie Schmitter Gilles Precigoux |
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Affiliation: | Unité de Biophysique Structurale, UMR 5471 CNRS, Université Bordeaux 1, Talence, France. |
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Abstract: | 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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Keywords: | circular dichroism ε‐subunit mitochondrial F1FO‐ATPase peptide synthesis |
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