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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Published in | Journal of peptide science Vol. 8; no. 7; pp. 365 - 372 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
01.07.2002
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Subjects | |
Online Access | Get full text |
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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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 content type line 23 ObjectType-Feature-2 |
ISSN: | 1075-2617 |
DOI: | 10.1002/psc.399 |