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Related Experiment Videos

Are membrane proteins "inside-out" proteins?

T J Stevens1, I T Arkin

  • 1Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, United Kingdom.

Proteins
|June 18, 1999
PubMed
Summary
This summary is machine-generated.

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The "inside-out" protein paradigm for membrane proteins is unfounded. Analysis shows residue hydrophobicity doesn't dictate location in transmembrane helical bundles, challenging existing models.

Area of Science:

  • Structural Biology
  • Biophysics
  • Membrane Protein Research

Background:

  • The prevailing model posits membrane proteins are
  • inside-out
  • with polar residues internally and apolar residues externally.
  • This contrasts with water-soluble proteins, which have apolar cores and polar surfaces.

Purpose of the Study:

  • To statistically test the
  • inside-out
  • paradigm for transmembrane alpha-helical proteins.
  • To investigate the correlation between residue accessibility and hydrophobicity within transmembrane helical bundles.

Main Methods:

  • Statistical analysis of accessible transmembrane alpha-helical structures.
  • Correlation analysis of individual residue and complete helix accessibility and hydrophobicity.

Related Experiment Videos

  • Comparative analysis with water-soluble helical bundles.

    • Main Results:

    • No significant correlation found between residue hydrophobicity and location within transmembrane helical bundles.
    • The hydrophilic vector of a helix is not a reliable predictor of solvent-exposed faces.
    • Both polar and hydrophobic residues exhibit no bias for interior or exterior positioning in transmembrane domains.
    • Control analysis of water-soluble proteins showed clear hydrophobicity-accessibility correlations.

    Conclusions:

    • The
    • inside-out
    • model for membrane proteins is not supported by current structural data.
    • Transmembrane helix packing is likely driven by van der Waals forces, not solely by hydrophobic/hydrophilic segregation.
    • Re-evaluation of membrane protein structure-