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Spatial organization and conformational peculiarities of the callatostatin family of neuropeptides
Author(s) -
Alieva I. N.,
Velieva L. I.,
Aliev D. I.,
Godjaev N. M.
Publication year - 2002
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.389
Subject(s) - pentapeptide repeat , conformational isomerism , chemistry , amino acid residue , stereochemistry , neuropeptide , conformational change , peptide , biophysics , biochemistry , peptide sequence , biology , molecule , organic chemistry , receptor , gene
The structures and conformational peculiarities of five members of the callatostatin family of neuropeptides, i.e. Leu‐ and Met‐callatostatins, ranging in size from 8 to 16 amino acid residues have been investigated by a theoretical conformational analysis method. A comparative analysis of the conformational flexibilities of Met‐callatostatin with those of the hydroxylated analogues, [Hyp 2 ]‐ and [Hyp 3 ]‐ Met‐callatostatin has been carried out. Helically packed C ‐terminal pentapeptide in the structure of all investigated Leu‐callatostatins are shown to be possible. The reason for the great number low‐energy conformers for the callatostatin N ‐terminus is discussed. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.