Sequence-specific 1H NMR assignments and secondary structure of a lipid-associating peptide from human ApoC-I: an NMR study of an amphipathic helix motif.

Abstract

The conformation of a synthetic peptide corresponding to residues 35-53 (SAKM-REWFSETFQKVKEKL) of human apolipoprotein C-I (57 amino acids) was studied by nuclear magnetic resonance and circular dichroism spectroscopy in water and in perdeuterated dodecylphosphocholine solution at 37 degrees C and pH 4.8. The proton resonances of the peptide in both solutions were assigned from TOCSY, NOESY and DQF-COSY experiments. In water solution, the peptide is predominantly "random", although nuclear Overhauser connectivity patterns and H alpha secondary shifts show a threshold population of nascent helical conformers. Upon the addition of 40-fold molar excess dodecylphosphocholine to the water solution, the peptide adopts a helical structure that extends throughout the sequence.