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== | ==GRAMICIDIN A IN HYDRATED DMPC BILAYERS, SOLID STATE NMR== | ||
<StructureSection load='1mag' size='340' side='right'caption='[[1mag]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1mag]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MAG FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR, 1 model</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DLE:D-LEUCINE'>DLE</scene>, <scene name='pdbligand=DVA:D-VALINE'>DVA</scene>, <scene name='pdbligand=ETA:ETHANOLAMINE'>ETA</scene>, <scene name='pdbligand=FVA:N-FORMYL-L-VALINE'>FVA</scene>, <scene name='pdbligand=PRD_000150:GRAMICIDIN+A'>PRD_000150</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=1mag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mag OCA], [https://pdbe.org/1mag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mag RCSB], [https://www.ebi.ac.uk/pdbsum/1mag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mag ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | 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. | ||
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<ref>PMID:8810522</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1mag" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Gramicidin|Gramicidin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Brevibacillus brevis]] | |||
[[Category: Large Structures]] | |||
[[Category: Cross TA]] | |||
[[Category: Ketchem RR]] | |||
[[Category: Roux B]] | |||
Latest revision as of 07:43, 17 October 2024
GRAMICIDIN A IN HYDRATED DMPC BILAYERS, SOLID STATE NMRGRAMICIDIN A IN HYDRATED DMPC BILAYERS, SOLID STATE NMR
Structural highlights
Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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