Study of the yeast Saccharomyces cerevisiae F 1 F O ‐ATPase ε‐subunit

Abstract The yeast Saccharomyces cerevisiae F 1 F O ‐ATPase ε‐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 ε‐subunit. The strong propensity of the protein to produce few soluble...

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Published inJournal of peptide science Vol. 8; no. 7; pp. 365 - 372
Main Authors Aznar‐Derunes, Céline, Manigand, Claude, Picard, Philippe, Dautant, Alain, Goetz, Michael, Schmitter, Jean‐Marie, Precigoux, Gilles
Format Journal Article
LanguageEnglish
Published 01.07.2002
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Summary:Abstract The yeast Saccharomyces cerevisiae F 1 F O ‐ATPase ε‐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 ε‐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 m M sodium dodecyl sulphate is required for helical folding. In both solvents at acidic pH, the ε‐subunit is soluble and monomeric. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.
ISSN:1075-2617
1099-1387
DOI:10.1002/psc.399