Solution NMR structure of a model class A (apolipoprotein) amphipathic alpha helical peptide.

Academic Article

Abstract

  • To better understand the structural determinants of the physical-chemical and the biological properties of Ac-18A-NH(2) (acetyl-AspTrpLeuLysAlaPheTyrAspLysValAlaGluLysLeuLysGluAlaPhe-amide), we have determined its structure in 50% (v/v) trifluroethanol (TFE-d(3))/water mixture (5 mM potassium phosphate, pH 5.5, 310K) using two-dimensional proton NMR spectroscopy. Stereospecific assignments have been made for C(beta)H protons (all the residues except Ala and Val) and gammaCH(3) (Val) groups. Nuclear Overhauser effects are observed between the nonpolar side chains spaced at (i) and (i + 4) position in the primary sequence, e.g., Trp2 and Phe6, and Phe6 and Val10. This suggests that in addition to N-terminal acetyl and C-terminal amide groups, the amphipathic alpha helical structure of Ac-18A-NH(2) is further stabilized by interactions between the hydrophobic residues on the nonpolar face of the helix.
  • Published In

  • Peptides  Journal
  • Keywords

  • Amino Acid Sequence, Apolipoproteins, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Peptide Fragments, Protein Conformation
  • Authorlist

  • Mishraa VK; Palgunachari MN; Anantharamaiah GM; Jones MK; Segrest JP; Krishna NR
  • Start Page

  • 567
  • End Page

  • 573
  • Volume

  • 22
  • Issue

  • 4