1r9v
From Proteopedia
(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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'''NMR Structure of a D,L-Alternating Dodecamer of Norleucine'''<br /> | '''NMR Structure of a D,L-Alternating Dodecamer of Norleucine'''<br /> | ||
==Overview== | ==Overview== | ||
| - | beta-Helix structures are of particular interest due to their capacity to | + | 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== | ==About this Structure== | ||
| - | 1R9V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1R9V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R9V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ion channel]] | [[Category: ion channel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:48:34 2008'' |
Revision as of 12:48, 21 February 2008
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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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