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A large number of modified amino acids other than the canonical amino acid residues can be found in natural products, especially antibiotics. The structure of these peptide-based compounds is investigated using modern two-dimensional
NMR
techniques. The automatic assignment of the 2D NMR proton spectra and consequent determination of the primary and 3D structure of peptides or small size proteins containing natural amino acids is nowadays routine. However, a deficiency in the ability to readily sequence peptides containing unnatural amino acids still remains and a great human effort and time is required. The experimental methods and the protocols of manual analysis of the data are described in the following sections.