2lny: Difference between revisions
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==ShB peptide structure bound to negatively charged lipid-bilayer after Molecular Dynamics refinement== | |||
<StructureSection load='2lny' size='340' side='right'caption='[[2lny]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2lny]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LNY FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</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=2lny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lny OCA], [https://pdbe.org/2lny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lny RCSB], [https://www.ebi.ac.uk/pdbsum/2lny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lny ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Elemental biological functions such as molecular signal transduction are determined by the dynamic interplay between polypeptides and the membrane environment. Determining such supramolecular arrangements poses a significant challenge for classical structural biology methods. We introduce an iterative approach that combines magic-angle spinning solid-state NMR spectroscopy and atomistic molecular dynamics simulations for the determination of the structure and topology of membrane-bound systems with a resolution and level of accuracy difficult to obtain by either method alone. Our study focuses on the Shaker B ball peptide that is representative for rapid N-type inactivating domains of voltage-gated K(+) channels, associated with negatively charged lipid bilayers. | |||
Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.,Weingarth M, Ader C, Melquiond AJ, Nand D, Pongs O, Becker S, Bonvin AM, Baldus M Biophys J. 2012 Jul 3;103(1):29-37. PMID:22828329<ref>PMID:22828329</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2lny" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Weingarth M]] | |||
Latest revision as of 05:47, 15 May 2024
ShB peptide structure bound to negatively charged lipid-bilayer after Molecular Dynamics refinement
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