title: A 400 MHz 1H NMR study of fortuitin, a natural linear lipopeptide.
abstract: Fortuitin is a linear acyl nonapeptide methyl ester in which all the peptide residues are hydrophobic. Its 400 MHz 1H NMR spectrum in pyridine-d5 has been assigned. In this solvent, its conformation is not random and seems to form a hairpin. Conformational equilibria exist in pyridine as well as in less polar solvents such as CDCl3 and CD2Cl2. As for other lipopeptides, conformation and self-association properties strongly depend on the polarity of the environment. These properties should be related to the interactions of lipopeptides with membranes and to their capacity to induce pore formation.
mesh_terms: D008074:Lipoproteins; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation
chemical_list: D008074:Lipoproteins; C038209:fortuitin