2n4n
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NMR structure for a 3-stranded parallel beta-sheet== | |
| + | <StructureSection load='2n4n' size='340' side='right'caption='[[2n4n]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2n4n]] 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=2N4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N4N FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4FU:(1R,2S)-CYCLOHEXANE-1,2-DICARBOXYLIC+ACID'>4FU</scene>, <scene name='pdbligand=4G6:2-METHYLPROPANE-1,2-DIAMINE'>4G6</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=DPR:D-PROLINE'>DPR</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=2n4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n4n OCA], [https://pdbe.org/2n4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n4n RCSB], [https://www.ebi.ac.uk/pdbsum/2n4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n4n ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We have examined whether parallel beta-sheet secondary structure becomes more stable as the number of beta-strands increases, via comparisons among peptides designed to adopt two- or three-stranded parallel beta-sheet conformations in aqueous solution. Our three-strand design is the first experimental model of a triple-stranded parallel beta-sheet. Analysis of the designed peptides by nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy supports the hypothesis that increasing the number of beta-strands, from two to three, increases the stability of the parallel beta-sheet. We present the first experimental evidence for cooperativity in the folding of a triple-stranded parallel beta-sheet, and we show how minimal model systems may enable experimental documentation of characteristic properties, such as CD spectra, of parallel beta-sheets. | ||
| - | + | Impact of Strand Number on Parallel beta-Sheet Stability.,Kung VM, Cornilescu G, Gellman SH Angew Chem Int Ed Engl. 2015 Nov 23;54(48):14336-9. doi: 10.1002/anie.201506448. , Epub 2015 Oct 12. PMID:26457984<ref>PMID:26457984</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Cornilescu | + | <div class="pdbe-citations 2n4n" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Cornilescu G]] | ||
| + | [[Category: Gellman SH]] | ||
| + | [[Category: Kung VM]] | ||
Current revision
NMR structure for a 3-stranded parallel beta-sheet
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