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

The yeast Saccharomyces cerevisiae F1FO-ATPase -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 -subunit. The strong propensity of the protein to produce few soluble dimeric species...

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Bibliographic Details
Published inJournal of peptide science Vol. 8; no. 7; pp. 365 - 372
Main Authors Aznar-Derunes, Celine, Picard, Claude Manigand Philippe, Dautant, Alain, Goetz, Michael, Schmitter, Jean-Marie, Precigoux, Gilles
Format Journal Article
LanguageEnglish
Published 01.07.2002
Subjects
Saccharomyces cerevisiae
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Summary:The yeast Saccharomyces cerevisiae F1FO-ATPase -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 -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 -subunit is soluble and monomeric.
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ISSN:1075-2617
DOI:10.1002/psc.399