1r9v
From Proteopedia
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| - | [[Image:1r9v.png|left|200px]] | ||
| - | + | ==NMR Structure of a D,L-Alternating Dodecamer of Norleucine== | |
| + | <StructureSection load='1r9v' size='340' side='right'caption='[[1r9v]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1r9v]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R9V FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOC:TERT-BUTYL+HYDROGEN+CARBONATE'>BOC</scene>, <scene name='pdbligand=DNE:D-NORLEUCINE'>DNE</scene>, <scene name='pdbligand=DNM:N-METHYL-D-NORLEUCINE'>DNM</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=NLO:O-METHYL-L-NORLEUCINE'>NLO</scene>, <scene name='pdbligand=PRD_000106:BOC-(D-NLE-L-NLE)4-D-NLE(METHYL)-L-NLE-D-NLE-L-NLE+METHYL+ESTER'>PRD_000106</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r9v OCA], [https://pdbe.org/1r9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r9v RCSB], [https://www.ebi.ac.uk/pdbsum/1r9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r9v ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:11373724</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1r9v" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Celda B]] |
| + | [[Category: Navarro E]] | ||
Current revision
NMR Structure of a D,L-Alternating Dodecamer of Norleucine
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