Abstract
Diverse methods have been developed and applied in the recent years to study interaction of transmembrane alpha-helices and often interaction of single transmembrane helices is followed on SDS-gels. Here we compare two measurements of the stability of a transmembrane helix-helix interaction, and the stability of the PsbF transmembrane helix dimer was determined in a biological membrane as well as in SDS. The observations described in this study demonstrate that the environment, in which a transmembrane helix interaction is studied, can be very critical and detergent properties can significantly influence transmembrane helix interactions, especially, when the transmembrane domain contains strongly polar residues.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Cell Membrane / metabolism*
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Cytochrome b Group / chemistry
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Cytochrome b Group / genetics
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Cytochrome b Group / metabolism
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Dimerization
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli
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Membrane Proteins / chemistry
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Membrane Proteins / genetics*
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Membrane Proteins / metabolism*
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Mutagenesis, Site-Directed*
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Mutation / genetics
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Peptide Fragments / chemistry
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Peptide Fragments / genetics*
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Peptide Fragments / metabolism*
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
Substances
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Cytochrome b Group
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Membrane Proteins
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Peptide Fragments
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Recombinant Fusion Proteins