Polar networks control oligomeric assembly in membranes

Chad D. Tatko, Vikas Nanda, James D. Lear, William F. DeGrado

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)4170-4171
Number of pages2
JournalJournal of the American Chemical Society
Volume128
Issue number13
DOIs
StatePublished - Apr 5 2006

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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