View source for 5uyo


==Solution NMR structure of the de novo mini protein HEEH_rd4_0097==
<StructureSection load='5uyo' size='340' side='right'caption='[[5uyo]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5uyo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UYO FirstGlance]. <br>
</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=5uyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uyo OCA], [https://pdbe.org/5uyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uyo RCSB], [https://www.ebi.ac.uk/pdbsum/5uyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uyo ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Proteins fold into unique native structures stabilized by thousands of weak interactions that collectively overcome the entropic cost of folding. Although these forces are "encoded" in the thousands of known protein structures, "decoding" them is challenging because of the complexity of natural proteins that have evolved for function, not stability. We combined computational protein design, next-generation gene synthesis, and a high-throughput protease susceptibility assay to measure folding and stability for more than 15,000 de novo designed miniproteins, 1000 natural proteins, 10,000 point mutants, and 30,000 negative control sequences. This analysis identified more than 2500 stable designed proteins in four basic folds-a number sufficient to enable us to systematically examine how sequence determines folding and stability in uncharted protein space. Iteration between design and experiment increased the design success rate from 6% to 47%, produced stable proteins unlike those found in nature for topologies where design was initially unsuccessful, and revealed subtle contributions to stability as designs became increasingly optimized. Our approach achieves the long-standing goal of a tight feedback cycle between computation and experiment and has the potential to transform computational protein design into a data-driven science.

Global analysis of protein folding using massively parallel design, synthesis, and testing.,Rocklin GJ, Chidyausiku TM, Goreshnik I, Ford A, Houliston S, Lemak A, Carter L, Ravichandran R, Mulligan VK, Chevalier A, Arrowsmith CH, Baker D Science. 2017 Jul 14;357(6347):168-175. doi: 10.1126/science.aan0693. PMID:28706065<ref>PMID:28706065</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Arrowsmith CH]]
[[Category: Baker D]]
[[Category: Carter L]]
[[Category: Chidyausiku TM]]
[[Category: Houliston S]]
[[Category: Lemak A]]
[[Category: Rocklin GJ]]