Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10798064 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2011 | 10 Pages |
Abstract
âºA 10-residue peptide from apolipopotein J adopts an amphipathic α-helical structure in the presence of dodecylphosphocholine micelle. âºSolution NMR structure of the 10-residue peptide in the presence of dodecylphosphocholine micelle has been determined. âºAbility of this peptide to associate with oxidized lipid helps explain its anti-inflammatory and anti-atherogenic properties.
Keywords
TPPIDSSroot–mean–square deviationRMSDNOENOESYCSIApoA-IDPCTOCSYnuclear magnetic resonanceApolipoprotein A-Iapolipoprotein Jnuclear overhauser effectNMRcircular dichroismsodium 2,2-dimethyl-2-silapentane-5-sulfonatechemical shift indexNOE spectroscopyNuclear magnetic resonance spectroscopyTotal correlation spectroscopytime proportional phase incrementationOxidized lipidPeptideIsothermal titration calorimetry
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Authors
Vinod K. Mishra, Mayakonda N. Palgunachari, Jason S. Hudson, Ronald Shin, Tamara D. Keenum, N. Rama Krishna, G.M. Anantharamaiah,