Polar networks control oligomeric assembly in membranes.
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.
Department of Chemistry, School of Medicine, University of Pennsylvania, Philadelphia, 19104, USA.
Chad D
CD
Tatko
Vikas
V
Nanda
James D
JD
Lear
William F
WF
Degrado
D000595:Amino Acid Sequence; D031541:Fluorescence Resonance Energy Transfer; D007700:Kinetics; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D012694:Serine / Q000737:chemistry; D013912:Threonine / Q000737:chemistry; D014461:Ultracentrifugation
D008565:Membrane Proteins; D010455:Peptides; D013912:Threonine; D012694:Serine