Abstract
The potentialities of solution-conformational NMR analysis of peptides with fixed (or predominant) structures do not lag behind the X-ray method for crystals. An outstanding merit of NMR spectroscopy is its ability to provide a deep insight into the dynamic aspects of the molecular conformation and intra- and intermolecular interactions in solution. The application of the NMR technique is illustrated by a conformational study of the cyclododecadepsipeptide valinomycin. The spatial structures of the larger linear peptides and small proteins could also be studied by NMR through detection of contacts between the side chains of amino acid residues which, being remote in the primary structure, are brought into close proximity by folding of the backbone. Examples described in this study are aparnin (18 amino acid residues) isolated from honey-bee venom and neurotoxin 11 (61 residues) isolated from Central Asian cobra Naja naja oxiana.
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