|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==NMR Structure of a D,L Alternating pentadecamer of norleucine: double antiparallel beta-helix== | | ==NMR Structure of a D,L Alternating pentadecamer of norleucine: double antiparallel beta-helix== |
| - | <StructureSection load='1s1o' size='340' side='right'caption='[[1s1o]], [[NMR_Ensembles_of_Models | 5 NMR models]]' scene=''> | + | <StructureSection load='1s1o' size='340' side='right'caption='[[1s1o]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1s1o]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S1O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1s1o]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S1O FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r9v|1r9v]]</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_000109:BOC-L-NLE-(D-NLE-L-NLE)5-D-NLE(METHYL)-L-NLE-D-NLE-L-NLE+METHYL+ESTER'>PRD_000109</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1o OCA], [http://pdbe.org/1s1o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s1o RCSB], [http://www.ebi.ac.uk/pdbsum/1s1o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s1o ProSAT]</span></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=1s1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1o OCA], [https://pdbe.org/1s1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s1o RCSB], [https://www.ebi.ac.uk/pdbsum/1s1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s1o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| Line 22: |
Line 22: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Celda, B]] | + | [[Category: Celda B]] |
| - | [[Category: Fennude, E]] | + | [[Category: Fennude E]] |
| - | [[Category: Navarro, E]] | + | [[Category: Navarro E]] |
| - | [[Category: Beta-helix]]
| + | |
| - | [[Category: De novo protein]]
| + | |
| - | [[Category: Gramicidin]]
| + | |
| - | [[Category: L-alternating]]
| + | |
| - | [[Category: Norleucine]]
| + | |
| Structural highlights
1s1o is a 2 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | Solution NMR |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Publication Abstract from PubMed
Conformational characteristics of alternating D,L linear peptides are of particular interest because of their capacity to form transmembrane channels with different transport properties, as some natural antibiotics do. Single- and double-stranded beta-helical structures are common for alternating D,L peptides. The stability of the beta-helix depends on several structural factors, such as the backbone peptide length, type and position of side chains, and nature of terminal groups. The NMR and molecular dynamics solution conformation of a synthetic alternating D,L-oligopeptide with 15 norleucines (XVMe) has been used as a model to get insight in to the conformational features of double-stranded beta-helix structures. The NH chemical shift values (delta(NH)) and long-range nuclear Overhauser effects (NOE) cross peaks, in particular interstrand connectivities, clearly point to an antiparallel double-stranded beta-helix for the XVMe major conformation in solution. An extensive set of distances (from NOE cross peaks) and H-bonds (from delta(NH)) has been included in the molecular dynamics calculations. The experimental NMR data and theoretical calculations clearly indicate that the most probable conformation of XVMe in solution is a double-strand antiparallel beta(5.6) increasing decreasing-helix structure.
Solution structure of a D,L-alternating oligonorleucine as a model of double-stranded antiparallel beta-helix.,Navarro E, Fenude E, Celda B Biopolymers. 2002 Aug 5;64(4):198-209. PMID:12115137[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Navarro E, Fenude E, Celda B. Solution structure of a D,L-alternating oligonorleucine as a model of double-stranded antiparallel beta-helix. Biopolymers. 2002 Aug 5;64(4):198-209. PMID:12115137 doi:http://dx.doi.org/10.1002/bip.10172
|
