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'''Unreleased structure'''


The entry 6gwx is ON HOLD
==Stabilising and Understanding a Miniprotein by Rational Design.==
<StructureSection load='6gwx' size='340' side='right'caption='[[6gwx]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6gwx]] 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=6GWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GWX FirstGlance]. <br>
</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=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=6gwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gwx OCA], [https://pdbe.org/6gwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gwx RCSB], [https://www.ebi.ac.uk/pdbsum/6gwx PDBsum], [https://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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6gwx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus mutans]]
[[Category: Baker EG]]
[[Category: Crump MP]]
[[Category: Nicol D]]
[[Category: Porter Goff KL]]
[[Category: Samphire JL]]
[[Category: Williams C]]
[[Category: Woolfson DN]]
[[Category: Zieleniewski FL]]
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