Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4595
Title: Metal ion effects on cis/trans isomerization of proline residues in short chain peptides in solution
Authors: Gaggelli, Elena 
N., D'Amelio
Gaggelli, Nicola 
Valensin, Gianni 
Issue Date: 2001
Project: None 
Journal: CHEMBIOCHEM
Abstract: 
The-effect of capper(II) ions on the probabilities of existence of the four detectable conformers of the tetrapeptide Tyr-Pro-Phe-Pro (beta -casomorphin 4) in [H-2(6)]DMSO was investigated by H-1 NMR Spectroscopy. Integration of the Phe-NH signals provided the relative populations in the free state as tt/tc/ct/cc = 28.34.29:9 at 293 K (c = cis, t = trans). Copper(ii) was shown to bind to all four isomers, yielding complexes with two different structures, depending on the conformation of Pro(2). The interpretation of paramagnetic relaxation rates of Pro(2)-H alpha signals provided the corresponding isomeric probabilities in the metal-bound state as 13:36:20:31. The observed stabilization of the conformation with the lowest probability of-existence (cc) may be relevant for the biological role of copper and other metal ions.
Description: 
18512
URI: http://hdl.handle.net/20.500.12779/4595
ISSN: 1439-4227
DOI: 10.1002/1439-7633(20010803)2:7/8<524
Appears in Collections:Publications

Show full item record

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.