Abstract
Cytochrome c₅ of pressure-sensitive Shewanella livingstonensis (SL cytc₅) exhibits lower thermal stability than a highly homologous counterpart of pressure-tolerant Shewanella violacea. This stability difference is due to an enthalpic effect that can be attributed to the amino acid residue at position 50 (Leu or Lys). These cytc₅ proteins are appropriate materials for understanding the protein stability mechanism.
MeSH terms
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Amino Acid Sequence
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Aquatic Organisms / chemistry
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Aquatic Organisms / enzymology*
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Cloning, Molecular
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Cytochrome c Group / chemistry*
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Cytochrome c Group / genetics
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Cytochrome c Group / metabolism
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Enzyme Stability
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Escherichia coli
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Models, Molecular
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Molecular Sequence Data
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Phase Transition
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Plasmids
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Pressure
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Protein Structure, Secondary
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Recombinant Proteins / chemistry*
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Shewanella / chemistry
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Shewanella / enzymology*
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Temperature
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Thermodynamics
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Transformation, Bacterial
Substances
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Bacterial Proteins
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Cytochrome c Group
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Recombinant Proteins
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cytochrome C5