Abstract
Understanding how the lipid environment influences transmembrane helix association requires thermodynamic measurements that can be interpreted in terms of specific chemical interactions. We have used Förster resonance energy transfer to measure dimerization of the glycophorin A transmembrane helix in detergent micelles. The observed Kd is at least two orders of magnitude weaker in sodium dodecyl sulfate than it is in zwitterionic detergents. In contrast, neither dimerization nor the detergent affects the secondary structure of the glycophorin A helix as measured by far-UV circular dichroism. These measurements support a long standing assumption about the glycophorin A transmembrane domain, that detergents uncouple helix formation from helix dimerization. The approach is applicable to a variety of systems in diverse environments, extending our ability to measure how interactions with complex solvents affect the thermodynamics of oligomerization.
Copyright 1999 Academic Press.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Butyrates / chemistry
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Butyrates / pharmacology
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Circular Dichroism
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Detergents / chemistry
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Detergents / pharmacology*
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Dimerization
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Energy Transfer
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Fluorescent Dyes
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Glycophorins / chemistry*
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Glycophorins / metabolism*
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Humans
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Kinetics
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Micelles
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Molecular Sequence Data
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Peptide Fragments / chemistry*
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Peptide Fragments / metabolism*
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Phosphorylcholine / analogs & derivatives
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Phosphorylcholine / chemistry
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Phosphorylcholine / pharmacology
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Protein Structure, Secondary
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Quaternary Ammonium Compounds / chemistry
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Quaternary Ammonium Compounds / pharmacology
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Sodium Dodecyl Sulfate / chemistry
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Sodium Dodecyl Sulfate / pharmacology
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Solvents
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Spectrometry, Fluorescence
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Thermodynamics
Substances
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(N-dodecyl-N,N-dimethylammonio)butyric acid
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Butyrates
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Detergents
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Fluorescent Dyes
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Glycophorins
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Micelles
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Peptide Fragments
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Quaternary Ammonium Compounds
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Solvents
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Phosphorylcholine
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Sodium Dodecyl Sulfate
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dodecylphosphocholine