5lo3
From Proteopedia
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<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=5lo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lo3 OCA], [http://pdbe.org/5lo3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lo3 RCSB], [http://www.ebi.ac.uk/pdbsum/5lo3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lo3 ProSAT]</span></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=5lo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lo3 OCA], [http://pdbe.org/5lo3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lo3 RCSB], [http://www.ebi.ac.uk/pdbsum/5lo3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lo3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Miniproteins simplify the protein-folding problem, allowing the dissection of forces that stabilize protein structures. Here we describe PPalpha-Tyr, a designed peptide comprising an alpha-helix buttressed by a polyproline II helix. PPalpha-Tyr is water soluble and monomeric, and it unfolds cooperatively with a midpoint unfolding temperature (TM) of 39 degrees C. NMR structures of PPalpha-Tyr reveal proline residues docked between tyrosine side chains, as designed. The stability of PPalpha is sensitive to modifications in the aromatic residues: replacing tyrosine with phenylalanine, i.e., changing three solvent-exposed hydroxyl groups to protons, reduces the TM to 20 degrees C. We attribute this result to the loss of CH-pi interactions between the aromatic and proline rings, which we probe by substituting the aromatic residues with nonproteinogenic side chains. In analyses of natural protein structures, we find a preference for proline-tyrosine interactions over other proline-containing pairs, and observe abundant CH-pi interactions in biologically important complexes between proline-rich ligands and SH3 and similar domains. | ||
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| + | Engineering protein stability with atomic precision in a monomeric miniprotein.,Baker EG, Williams C, Hudson KL, Bartlett GJ, Heal JW, Porter Goff KL, Sessions RB, Crump MP, Woolfson DN Nat Chem Biol. 2017 Jul;13(7):764-770. doi: 10.1038/nchembio.2380. Epub 2017 May , 22. PMID:28530710<ref>PMID:28530710</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5lo3" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 09:59, 3 August 2017
Engineering protein stability with atomic precision in a monomeric miniprotein
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