1mag
From Proteopedia
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| - | [[Image:1mag.jpg|left|200px]] | + | [[Image:1mag.jpg|left|200px]] |
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| - | '''GRAMICIDIN A IN HYDRATED DMPC BILAYERS, SOLID STATE NMR''' | + | {{Structure |
| + | |PDB= 1mag |SIZE=350|CAPTION= <scene name='initialview01'>1mag</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FOR:FORMYL GROUP'>FOR</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''GRAMICIDIN A IN HYDRATED DMPC BILAYERS, SOLID STATE NMR''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MAG is a [ | + | 1MAG 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=1MAG OCA]. |
==Reference== | ==Reference== | ||
| - | Macromolecular structural elucidation with solid-state NMR-derived orientational constraints., Ketchem RR, Lee KC, Huo S, Cross TA, J Biomol NMR. 1996 Jul;8(1):1-14. PMID:[http:// | + | Macromolecular structural elucidation with solid-state NMR-derived orientational constraints., Ketchem RR, Lee KC, Huo S, Cross TA, J Biomol NMR. 1996 Jul;8(1):1-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8810522 8810522] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Cross, T A.]] | [[Category: Cross, T A.]] | ||
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[[Category: FOR]] | [[Category: FOR]] | ||
[[Category: 2h nmr]] | [[Category: 2h nmr]] | ||
| - | [[Category: gramicidin | + | [[Category: gramicidin some]] |
| - | [[Category: ion | + | [[Category: ion channel]] |
[[Category: membrane ion channel]] | [[Category: membrane ion channel]] | ||
[[Category: membrane protein structure]] | [[Category: membrane protein structure]] | ||
| - | [[Category: oriented | + | [[Category: oriented bilayer]] |
[[Category: peptide antibiotic]] | [[Category: peptide antibiotic]] | ||
[[Category: side chain conformation]] | [[Category: side chain conformation]] | ||
| - | ''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 12:41:01 2008'' |
Revision as of 10:41, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
GRAMICIDIN A IN HYDRATED DMPC BILAYERS, SOLID STATE NMR
Overview
The complete structure determination of a polypeptide in a lipid bilayer environment is demonstrated built solely upon orientational constraints derived from solid-state NMR observations. Such constraints are obtained from isotopically labeled samples uniformly aligned with respect to the B(0) field. Each observation constrains the molecular frame with respect to B(0) and the bilayer normal, which are arranged to be parallel. These constraints are not only very precise ( a few tenths of a degree), but also very accurate. This is clearly demonstrated as the backbone structure is assembled sequentially and the i to i + 6 hydrogen bonds in this structure of the gramicidin channel are shown on average to be within 0.5 A of ideal geometry. Similarly, the side chains are assembled independently and in a radial direction from the backbone. The lack of considerable atomic overlap between side chains also demonstrates the accuracy of the constraints. Through this complete structure, solid-state NMR is demonstrated as an approach for determining three-dimensional macromolecular structure.
About this Structure
1MAG is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Macromolecular structural elucidation with solid-state NMR-derived orientational constraints., Ketchem RR, Lee KC, Huo S, Cross TA, J Biomol NMR. 1996 Jul;8(1):1-14. PMID:8810522
Page seeded by OCA on Thu Mar 20 12:41:01 2008
