Reference: Aznar-Derunes C, et al. (2002) Study of the yeast Saccharomyces cerevisiae F1F0-ATPase epsilon-subunit. J Pept Sci 8(7):365-72

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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.

Reference Type
Journal Article
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Aznar-Derunes C, Manigand C, Picard P, Dautant A, Goetz M, Schmitter JM, Precigoux G
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