Premium
Study of the yeast Saccharomyces cerevisiae F 1 F O ‐ATPase ε‐subunit
Author(s) -
AznarDerunes Céline,
Manigand Claude,
Picard Philippe,
Dautant Alain,
Goetz Michael,
Schmitter JeanMarie,
Precigoux Gilles
Publication year - 2002
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.399
Subject(s) - chemistry , saccharomyces cerevisiae , protein subunit , yeast , circular dichroism , monomer , chromatography , peptide , gel electrophoresis , sodium , mass spectrometry , molecular mass , size exclusion chromatography , biochemistry , crystallography , enzyme , polymer , organic chemistry , gene
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.