Circular dichroism conformational study of the chemotactic peptide formyl-L-methionyl-L-leucyl-L-phenylalanine.
The solution circular dichroism of the chemotactic agent formyl-L-methionyl-L-leucyl-L-phenylalanine was found to be highly solvent dependent. In relatively nonpolar solvents (fluoroalcohols) the circular dichroism is that characteristic of a folded conformation. In H2SO4 the tripeptide remains intact and displays a circular dichroism typical of highly solvated and totally disordered peptides. The order-to-disorder transition can be followed by addition of water to trifluoroethanol.
D002630:Chemotactic Factors; D002942:Circular Dichroism; D008715:Methionine / Q000031:analogs & derivatives*; D009239:N-Formylmethionine / Q000031:analogs & derivatives*; D009240:N-Formylmethionine Leucyl-Phenylalanine; D009842:Oligopeptides; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet
D002630:Chemotactic Factors; D009842:Oligopeptides; D009239:N-Formylmethionine; D009240:N-Formylmethionine Leucyl-Phenylalanine; D008715:Methionine