title: High field NMR study of antibiotic peptides: 1H assignment of trichorzianine A1 spectra by 2D experiments.
abstract: A new antibiotic peptide, trichorzianine A1, was isolated from a culture of Trichoderma harzianum. It contains 19 residues, the N terminus is blocked by an acetyl group and the C terminus is tryptophanol. As a first part of the structural study of this new peptide, we here present the analysis of the 1H NMR spectrum accomplished by 2 DJ resolved and spin echo correlated spectroscopy.
mesh_terms: D000577:Amides; D000900:Anti-Bacterial Agents; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D054848:Peptaibols; D010455:Peptides
chemical_list: D000577:Amides; D000900:Anti-Bacterial Agents; D054848:Peptaibols; D010455:Peptides; C039715:trichorzianine