Spatial organization and conformational peculiarities of the callatostatin family of neuropeptides

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 confo...

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Bibliographic Details
Published in:Journal of peptide science 2002-08, Vol.8 (8), p.385-397
Main Authors: Alieva, I. N., Velieva, L. I., Aliev, D. I., Godjaev, N. M.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
callatostatin
Computer Simulation
conformation
conformational analysis
Models, Molecular
Molecular Sequence Data
neuropeptide
Neuropeptides - chemistry
Oligopeptides - chemistry
Peptide Fragments - chemistry
Protein Conformation
structure
Thermodynamics
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Summary: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, [Hyp2]‐ and [Hyp3]‐ 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.
ISSN:1075-2617
1099-1387
DOI:10.1002/psc.389