Study of the yeast Saccharomyces cerevisiae F1FO-ATPase ε-subunit

✍ Scribed by Céline Aznar-Derunes; Claude Manigand; Dr Philippe Picard; Alain Dautant; Michael Goetz; Jean-Marie Schmitter; Gilles Precigoux

• Publisher: John Wiley and Sons
• Year: 2002
• Tongue: English
• Weight: 165 KB
• Volume: 8
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/psc.399

✦ Synopsis

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 mM 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.