9ol9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Backbone-modified parallel beta hairpin (PBH): N-alpha-amino Phenylalanine at position 4== | |
| + | <StructureSection load='9ol9' size='340' side='right'caption='[[9ol9]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9ol9]] is a 2 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=9OL9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9OL9 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=4G6:2-METHYLPROPANE-1,2-DIAMINE'>4G6</scene>, <scene name='pdbligand=A1CCR:(2~{S})-2-diazanyl-3-phenyl-propanoic+acid'>A1CCR</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=DPR:D-PROLINE'>DPR</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=9ol9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ol9 OCA], [https://pdbe.org/9ol9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ol9 RCSB], [https://www.ebi.ac.uk/pdbsum/9ol9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ol9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Peptide backbone N-amination has emerged as a useful strategy to stabilize antiparallel beta-sheet structure. Here, we used circular dichroism and NMR to evaluate the impact of amide-to-hydrazide substitution on the folded population of a parallel beta-hairpin model. Outer-edge N-amination was well tolerated and resulted in enhanced stability relative to N-methylation. High-resolution NMR structures confirmed that the alpha-hydrazino acid residues adopt canonical parallel beta-strand torsions that are compatible with the formation of intraresidue C6 hydrogen bonds involving the hydrazide NH(2) group. | ||
| - | + | Impact of Strand Edge N-Amination on the Stability of a Parallel beta-Hairpin Fold.,Starnes SK, Horne WS, Del Valle JR J Org Chem. 2025 Nov 20. doi: 10.1021/acs.joc.5c02479. PMID:41264875<ref>PMID:41264875</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 9ol9" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Del Valle JR]] | ||
| + | [[Category: Horne WS]] | ||
| + | [[Category: Starnes SK]] | ||
Current revision
Backbone-modified parallel beta hairpin (PBH): N-alpha-amino Phenylalanine at position 4
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