2n8i
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| + | |||
==Solution NMR Structure of Designed Protein DA05, Northeast Structural Genomics Consortium (NESG) Target OR626== | ==Solution NMR Structure of Designed Protein DA05, Northeast Structural Genomics Consortium (NESG) Target OR626== | ||
<StructureSection load='2n8i' size='340' side='right' caption='[[2n8i]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2n8i' size='340' side='right' caption='[[2n8i]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| Line 6: | Line 7: | ||
<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=2n8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n8i OCA], [http://pdbe.org/2n8i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n8i RCSB], [http://www.ebi.ac.uk/pdbsum/2n8i PDBsum]</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=2n8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n8i OCA], [http://pdbe.org/2n8i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n8i RCSB], [http://www.ebi.ac.uk/pdbsum/2n8i PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Natural recombination combines pieces of preexisting proteins to create new tertiary structures and functions. We describe a computational protocol, called SEWING, which is inspired by this process and builds new proteins from connected or disconnected pieces of existing structures. Helical proteins designed with SEWING contain structural features absent from other de novo designed proteins and, in some cases, remain folded at more than 100 degrees C. High-resolution structures of the designed proteins CA01 and DA05R1 were solved by x-ray crystallography (2.2 angstrom resolution) and nuclear magnetic resonance, respectively, and there was excellent agreement with the design models. This method provides a new strategy to rapidly create large numbers of diverse and designable protein scaffolds. | ||
| + | |||
| + | Design of structurally distinct proteins using strategies inspired by evolution.,Jacobs TM, Williams B, Williams T, Xu X, Eletsky A, Federizon JF, Szyperski T, Kuhlman B Science. 2016 May 6;352(6286):687-90. doi: 10.1126/science.aad8036. PMID:27151863<ref>PMID:27151863</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2n8i" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:39, 1 June 2016
Solution NMR Structure of Designed Protein DA05, Northeast Structural Genomics Consortium (NESG) Target OR626
| |||||||||||
