[Contribution of NMR spectroscopy to the study of structure-function relations of proteins and peptides]

NMR spectroscopy provides a unique means to study molecular conformation, mechanisms of action and structure-function relationships for peptides and proteins in solution under conditions approaching those of their physiological environment. Development of NMR techniques, especially directed to the peptide and protein conformational analysis, is considered under the topics of two-level signal assignment and structural significance of homo- and heteronuclear spin-spin couplings. The results of NMR conformational analysis are presented for solution spatial structure of valinomy cin and gramicidin A antibiotics, honey-bee neurotoxin apamin, scorpion insectotoxin I5A and snake venom neurotoxins of "short" and "long" types. The structure-function relationships are discussed for these biologically active molecules.