8es1
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Backbone modifications in the inter-helix loop of designed miniprotein oPPalpha: deltaOrn10-11 turn== | |
| + | <StructureSection load='8es1' size='340' side='right'caption='[[8es1]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8es1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ES1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ES1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</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=8es1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8es1 OCA], [https://pdbe.org/8es1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8es1 RCSB], [https://www.ebi.ac.uk/pdbsum/8es1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8es1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The importance of beta-turns to protein folding has motivated extensive efforts to stabilize the motif with non-canonical backbone connectivity. Prior work has focused almost exclusively on turns between strands in a beta-sheet (i. e., hairpins). Turns in other structural contexts are also common in nature and have distinct conformational preferences; however, design principles for their mimicry remain poorly understood. Here, we report strategies that stabilize non-hairpin beta-turns through systematic evaluation of the impacts of backbone alteration on the high-resolution folded structure and folded stability of a helix-loop-helix prototype protein. Several well-established hairpin turn mimetics are shown detrimental to folded stability and/or hydrophobic core packing, while less-explored modification schemes that reinforce alternate turn types lead to improved stability and more faithful structural mimicry. Collectively, these results have implications in control over protein folding through chemical modification as well as the design of protein mimetics. | ||
| - | + | Protein Backbone Alteration in Non-Hairpin beta-Turns: Impacts on Tertiary Folded Structure and Folded Stability.,Harmon TW, Horne WS Chembiochem. 2023 Mar 15:e202300113. doi: 10.1002/cbic.202300113. PMID:36920327<ref>PMID:36920327</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8es1" style="background-color:#fffaf0;"></div> |
| - | [[Category: Harmon | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptococcus mutans]] | ||
| + | [[Category: Harmon TW]] | ||
| + | [[Category: Horne WS]] | ||
Revision as of 06:30, 7 April 2023
Backbone modifications in the inter-helix loop of designed miniprotein oPPalpha: deltaOrn10-11 turn
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