8g0x
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8g0x]] 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=8G0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8G0X FirstGlance]. <br> | <table><tr><td colspan='2'>[[8g0x]] 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=8G0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8G0X FirstGlance]. <br> | ||
| - | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=DPR:D-PROLINE'>DPR</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=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=8g0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8g0x OCA], [https://pdbe.org/8g0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8g0x RCSB], [https://www.ebi.ac.uk/pdbsum/8g0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8g0x ProSAT]</span></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=8g0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8g0x OCA], [https://pdbe.org/8g0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8g0x RCSB], [https://www.ebi.ac.uk/pdbsum/8g0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8g0x ProSAT]</span></td></tr> | ||
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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. | 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 | + | Protein Backbone Alteration in Non-Hairpin beta-Turns: Impacts on Tertiary Folded Structure and Folded Stability.,Harmon TW, Horne WS Chembiochem. 2023 Jun 1;24(11):e202300113. doi: 10.1002/cbic.202300113. Epub 2023 , Mar 30. PMID:36920327<ref>PMID:36920327</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
Backbone modifications in the inter-helix loop of designed miniprotein oPPalpha: Pro10DPro11 turn
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