1mxq
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(New page: 200px<br /><applet load="1mxq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mxq" /> '''Solution Structure of the Tachykinin Peptide...)
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Revision as of 19:40, 20 November 2007
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Solution Structure of the Tachykinin Peptide Eledoisin
Overview
Both the aqueous and the lipid-induced structure of eledoisin, an, undecapeptide of mollusk origin, have been studied by two-dimensional, proton nuclear magnetic resonance spectroscopy and distance geometry, calculations. Unambiguous nuclear magnetic resonance assignments of, protons have been made with the aid of correlation spectroscopy, experiments and nuclear Overhauser effect spectroscopy experiments. The, distance constraints obtained from the nuclear magnetic resonance data, have been utilized in a distance geometry algorithm to generate a family, of structures, which have been refined using restrained energy, minimization and dynamics. These data show that, while in water and, dimethyl sulfoxide, eledoisin prefers to be in an extended chain, conformation, whereas in the presence of perdeuterated, dodecylphosphocholine micelles, a membrane model system, helical, conformation is induced in the central core and C-terminal region (K4-M11), of the peptide. N terminus, though less defined, also displays some degree, of order and a possible turn structure. The conformation adopted by, eledoisin in the presence of dodecylphosphocholine micelles is similar to, the structural motif typical of neurokinin-2 selective agonists and with, that reported for kassinin in hydrophobic environment.
About this Structure
1MXQ is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Solution structure of the tachykinin peptide eledoisin., Grace RC, Chandrashekar IR, Cowsik SM, Biophys J. 2003 Jan;84(1):655-64. PMID:12524318
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