[An approach to the problem of the structuro-functional organization of natural peptides].
Theory and computational scheme of three-dimensional structure and dynamic conformational properties of naturally occurring peptides are proposed basing on a known amino acid sequence. The diverse biological activity of a low-molecular peptide is shown to arise from a restricted number of preferable spatial structures which may occur under physiological conditions. Each particular function of an oligopeptide is connected to a definite spatial structure, belonging to the set of low-energy conformations from one biological activity of a peptide shift of the conformational equilibrium caused by a change of environmental conditions. This shift is provided for by specific intramolecular interactions, alternative in their nature, which stabilize a particular structure. An approach is suggested which enables to construct a synthetic analog with the predetermined physiologically active conformation, prior to all chemical and biological tests.
D000595:Amino Acid Sequence; D000818:Animals; D003701:Delta Sleep-Inducing Peptide; D006801:Humans; D008958:Models, Molecular; D009419:Nerve Tissue Proteins; D009842:Oligopeptides; D010455:Peptides; D011487:Protein Conformation
D009419:Nerve Tissue Proteins; D009842:Oligopeptides; D010455:Peptides; D003701:Delta Sleep-Inducing Peptide
Podkhod k resheniiu problemy strukturno-funktsional'noĭ organizatsii prirodnykh peptidov.