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6gwx
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Stabilising and Understanding a Miniprotein by Rational Design.== | |
| + | <StructureSection load='6gwx' size='340' side='right'caption='[[6gwx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6gwx]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GWX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GWX FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5lo2|5lo2]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gwx OCA], [http://pdbe.org/6gwx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gwx RCSB], [http://www.ebi.ac.uk/pdbsum/6gwx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gwx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Miniproteins reduce the complexity of the protein-folding problem allowing systematic studies of contributions to protein folding and stabilization. Here, we describe the rational redesign of a miniprotein, PPalpha, comprising a polyproline II helix, a loop, and an alpha helix. The redesign provides a de novo framework for interrogating noncovalent interactions. Optimized PPalpha has significantly improved thermal stability with a midpoint unfolding temperature ( TM) of 51 degrees C. Its nuclear magnetic resonance structure indicates a density of stabilizing noncovalent interactions that is higher than that of the parent peptide, specifically an increased number of CH-pi interactions. In part, we attribute this to improved long-range electrostatic interactions between the two helical elements. We probe further sequence-stability relationships in the miniprotein through a series of rational mutations. | ||
| - | + | Stabilizing and Understanding a Miniprotein by Rational Redesign.,Porter Goff KL, Nicol D, Williams C, Crump MP, Zieleniewski F, Samphire JL, Baker EG, Woolfson DN Biochemistry. 2019 Jul 8. doi: 10.1021/acs.biochem.9b00067. PMID:31251570<ref>PMID:31251570</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6gwx" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Baker, E G]] | ||
| + | [[Category: Crump, M P]] | ||
| + | [[Category: Goff, K L.Porter]] | ||
| + | [[Category: Nicol, D]] | ||
| + | [[Category: Samphire, J L]] | ||
| + | [[Category: Williams, C]] | ||
| + | [[Category: Woolfson, D N]] | ||
| + | [[Category: Zieleniewski, F L]] | ||
| + | [[Category: Designed miniprotein ch-pi interactions weak non-covalent interactions in protiens solution structure proline-tyrosine interaction]] | ||
| + | [[Category: Structural protein]] | ||
Revision as of 05:41, 10 July 2019
Stabilising and Understanding a Miniprotein by Rational Design.
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Categories: Large Structures | Baker, E G | Crump, M P | Goff, K L.Porter | Nicol, D | Samphire, J L | Williams, C | Woolfson, D N | Zieleniewski, F L | Designed miniprotein ch-pi interactions weak non-covalent interactions in protiens solution structure proline-tyrosine interaction | Structural protein
