6gwx: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "6gwx" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
The | ==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]] | |||
