6d37
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Trp-cage tr16b R16Nva : Elimination of pH Dependent Interactions== | |
| + | <StructureSection load='6d37' size='340' side='right'caption='[[6d37]], [[NMR_Ensembles_of_Models | 32 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6d37]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D37 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=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NVA:NORVALINE'>NVA</scene></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=6d37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d37 OCA], [http://pdbe.org/6d37 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d37 RCSB], [http://www.ebi.ac.uk/pdbsum/6d37 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d37 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Trp-cage, an 18-20 residue miniprotein, has emerged as a primary test system for evaluating computational fold prediction and folding rate determination efforts. As it turns out, a number of stabilizing interactions in the Trp-cage folded state have a strong pH dependence; all prior Trp-cage mutants have been destabilized under carboxylate-protonating conditions. Notable among the pH dependent stabilizing interactions within the Trp-cage are: (1) an Asp as the helix N-cap, (2) an H-bonded Asp9/Arg16 salt bridge, (3) an interaction between the chain termini which are in close spatial proximity, and (4) additional side chain interactions with Asp9. In the present study, we have prepared Trp-cage species that are significantly more stable at pH 2.5 (rather than 7) and quantitated the contribution of each interaction listed above. The Trp-cage structure remains constant with the pH change. The study has also provided measures of the stabilizing contribution of indole ring shielding from surface exposure and the destabilizing effects of an ionized Asp at the C-terminus of an alpha-helix. | ||
| - | + | Reversing the typical pH stability profile of the Trp-cage.,Graham KA, Byrne A, Son R, Andersen NH Biopolymers. 2019 Mar;110(3):e23260. doi: 10.1002/bip.23260. Epub 2019 Feb 19. PMID:30779444<ref>PMID:30779444</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6d37" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Andersen, N H]] | ||
[[Category: Byrne, A]] | [[Category: Byrne, A]] | ||
| - | [[Category: | + | [[Category: Circular permutant]] |
| + | [[Category: De novo protein]] | ||
| + | [[Category: Microprotein]] | ||
| + | [[Category: Miniprotein]] | ||
| + | [[Category: Trp-cage]] | ||
Revision as of 11:55, 13 March 2019
Trp-cage tr16b R16Nva : Elimination of pH Dependent Interactions
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