Polar networks control oligomeric assembly in membranes

J Am Chem Soc. 2006 Apr 5;128(13):4170-1. doi: 10.1021/ja055561a.


Polar interactions have a profound influence on membrane stability and structure. A membrane-solubilized GCN4 peptide, MS-1, is used to study the impact of polar networks. Amide functionalities from amino acid side chains have been shown to promote peptide oligomerization, but lacked specificity. Herein, the hydrogen bonding interactions of an Asn side chain are coupled with the hydroxyl of Ser or Thr to generate a polar network. Analytical ultracentrifugation and fluorescence resonance energy transfer studies indicate that a trimer assembly is established where each membrane-embedded hydrogen bond contributes 1 kcal mol-1.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Fluorescence Resonance Energy Transfer
  • Kinetics
  • Membrane Proteins / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Protein Folding
  • Serine / chemistry
  • Threonine / chemistry
  • Ultracentrifugation


  • Membrane Proteins
  • Peptides
  • Threonine
  • Serine