Probing helix formation in unsolvated peptides.
Ion mobility measurements have been used to examine helix formation in unsolvated glycine-based peptides containing three alanine residues. Nine sequence isomers of Ac-[12G3A]K+H(+) were studied (Ac = acetyl, G = glycine, A = alanine, and K = lysine). The amount of helix present for each peptide was examined using two metrics, and it is strongly dependent on the proximity and the location of the alanine residues. Peptides with three adjacent alanines have the highest helix abundances, and those with well-separated alanines have the lowest. The helix abundances for most of the peptides can be fit reasonably well using a modified Lifson-Roig theory. However, Lifson-Roig theory fails to account for several key features of the experimental results. The most likely explanation for the correlation between helix abundances and the number of adjacent alanines is that neighboring alanines promote helix nucleation.
Breaux
Gary A
GA
Chemistry Department, Indiana University, 800 East Kirkwood Avenue, Bloomington, IN 47405-7102, USA.
Jarrold
Martin F
MF
D000409:Alanine / Q000737:chemistry; D000595:Amino Acid Sequence; D005998:Glycine / Q000737:chemistry; D008239:Lysine / Q000737:chemistry; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013816:Thermodynamics
D010455:Peptides; D008239:Lysine; D000409:Alanine; D005998:Glycine