1s1o
From Proteopedia
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| - | [[Image:1s1o.jpg|left|200px]] | + | [[Image:1s1o.jpg|left|200px]] |
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| - | '''NMR Structure of a D,L Alternating pentadecamer of norleucine: double antiparallel beta-helix''' | + | {{Structure |
| + | |PDB= 1s1o |SIZE=350|CAPTION= <scene name='initialview01'>1s1o</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=BOC:TERT-BUTYL HYDROGEN CARBONATE'>BOC</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NMR Structure of a D,L Alternating pentadecamer of norleucine: double antiparallel beta-helix''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1S1O is a [ | + | 1S1O is a [[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=1S1O OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12115137 12115137] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Celda, B.]] | [[Category: Celda, B.]] | ||
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[[Category: norleucine]] | [[Category: norleucine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:59:14 2008'' |
Revision as of 11:59, 20 March 2008
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NMR Structure of a D,L Alternating pentadecamer of norleucine: double antiparallel beta-helix
Overview
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.
About this Structure
1S1O is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 13:59:14 2008
Categories: Protein complex | Celda, B. | Fennude, E. | Navarro, E. | BOC | Beta-helix | D | Gramicidin | L-alternating | Norleucine
