1r9v
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(New page: 200px<br /><applet load="1r9v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r9v" /> '''NMR Structure of a D,L-Alternating Dodecamer...)
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Revision as of 20:17, 24 November 2007
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NMR Structure of a D,L-Alternating Dodecamer of Norleucine
Overview
beta-Helix structures are of particular interest due to their capacity to, form transmembrane channels with different transport properties. However, the relatively large number of beta-helices configurations does not allow, a direct conformational analysis of beta-helical oligopeptides. A, synthetic alternating D,L-oligopeptide with twelve norleucines (XIIMe) has, been used as a model to get insight in the conformational features of, beta-helix structures. The spatial configuration of XIIMe in solution has, been determined by NMR. An extensive set of distances (nuclear Overhauser, effect) and dihedral (J coupling constants) constraints have been included, in molecular dynamics calculations. The NMR experimental data and, theoretical calculations clearly indicate that the XIIMe adopts a single, beta(4.4)-helix-type conformation in nonpolar solvents.
About this Structure
1R9V is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Solution NMR structure of a D,L-alternating oligonorleucine as a model of beta-helix., Navarro E, Tejero R, Fenude E, Celda B, Biopolymers. 2001 Aug;59(2):110-9. PMID:11373724
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