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Polar Networks Control Oligomeric Assembly in Membranes

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

Department of Chemistry and Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104

J. Am. Chem. Soc., 2006, 128 (13), pp 4170–4171

DOI: 10.1021/ja055561a

Publication Date (Web): March 10, 2006

Section:

General Biochemistry

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.

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