6nuk

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Current revision (14:49, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6nuk' size='340' side='right'caption='[[6nuk]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
<StructureSection load='6nuk' size='340' side='right'caption='[[6nuk]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6nuk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NUK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NUK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6nuk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NUK FirstGlance]. <br>
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</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=6nuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nuk OCA], [http://pdbe.org/6nuk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nuk RCSB], [http://www.ebi.ac.uk/pdbsum/6nuk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nuk ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6nuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nuk OCA], [https://pdbe.org/6nuk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nuk RCSB], [https://www.ebi.ac.uk/pdbsum/6nuk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nuk ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Online citizen science projects such as GalaxyZoo(1), Eyewire(2) and Phylo(3) have proven very successful for data collection, annotation and processing, but for the most part have harnessed human pattern-recognition skills rather than human creativity. An exception is the game EteRNA(4), in which game players learn to build new RNA structures by exploring the discrete two-dimensional space of Watson-Crick base pairing possibilities. Building new proteins, however, is a more challenging task to present in a game, as both the representation and evaluation of a protein structure are intrinsically three-dimensional. We posed the challenge of de novo protein design in the online protein-folding game Foldit(5). Players were presented with a fully extended peptide chain and challenged to craft a folded protein structure and an amino acid sequence encoding that structure. After many iterations of player design, analysis of the top-scoring solutions and subsequent game improvement, Foldit players can now-starting from an extended polypeptide chain-generate a diversity of protein structures and sequences that encode them in silico. One hundred forty-six Foldit player designs with sequences unrelated to naturally occurring proteins were encoded in synthetic genes; 56 were found to be expressed and soluble in Escherichia coli, and to adopt stable monomeric folded structures in solution. The diversity of these structures is unprecedented in de novo protein design, representing 20 different folds-including a new fold not observed in natural proteins. High-resolution structures were determined for four of the designs, and are nearly identical to the player models. This work makes explicit the considerable implicit knowledge that contributes to success in de novo protein design, and shows that citizen scientists can discover creative new solutions to outstanding scientific challenges such as the protein design problem.
 
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De novo protein design by citizen scientists.,Koepnick B, Flatten J, Husain T, Ford A, Silva DA, Bick MJ, Bauer A, Liu G, Ishida Y, Boykov A, Estep RD, Kleinfelter S, Norgard-Solano T, Wei L, Players F, Montelione GT, DiMaio F, Popovic Z, Khatib F, Cooper S, Baker D Nature. 2019 Jun 5. pii: 10.1038/s41586-019-1274-4. doi:, 10.1038/s41586-019-1274-4. PMID:31168091<ref>PMID:31168091</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 6nuk" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Synthetic construct sequences]]
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[[Category: Synthetic construct]]
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[[Category: Baker, D]]
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[[Category: Baker D]]
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[[Category: Bick, M J]]
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[[Category: Bick MJ]]
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[[Category: DiMaio, F]]
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[[Category: DiMaio F]]
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[[Category: Koepnick, B]]
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[[Category: Koepnick B]]
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[[Category: Norgard-Solano, T]]
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[[Category: Norgard-Solano T]]
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[[Category: De novo protein]]
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[[Category: Foldit]]
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Current revision

De novo designed protein Ferredog-Diesel

PDB ID 6nuk

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