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1uao
From Proteopedia
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| - | [[Image:1uao.gif|left|200px]]<br /><applet load="1uao" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1uao" /> | ||
| - | '''NMR Structure of designed protein, Chignolin, consisting of only ten amino acids (Ensembles)'''<br /> | ||
| - | == | + | ==NMR Structure of designed protein, Chignolin, consisting of only ten amino acids (Ensembles)== |
| + | <StructureSection load='1uao' size='340' side='right'caption='[[1uao]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1uao]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UAO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UAO FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1uao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uao OCA], [https://pdbe.org/1uao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uao RCSB], [https://www.ebi.ac.uk/pdbsum/1uao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uao ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
We have designed a peptide termed chignolin, consisting of only 10 amino acid residues (GYDPETGTWG), on the basis of statistics derived from more than 10,000 protein segments. The peptide folds into a unique structure in water and shows a cooperative thermal transition, both of which may be hallmarks of a protein. Also, the experimentally determined beta-hairpin structure was very close to what we had targeted. The performance of the short peptide not only implies that the methodology employed here can contribute toward development of novel techniques for protein design, but it also yields insights into the raison d'etre of an autonomous element involved in a natural protein. This is of interest for the pursuit of folding mechanisms and evolutionary processes of proteins. | We have designed a peptide termed chignolin, consisting of only 10 amino acid residues (GYDPETGTWG), on the basis of statistics derived from more than 10,000 protein segments. The peptide folds into a unique structure in water and shows a cooperative thermal transition, both of which may be hallmarks of a protein. Also, the experimentally determined beta-hairpin structure was very close to what we had targeted. The performance of the short peptide not only implies that the methodology employed here can contribute toward development of novel techniques for protein design, but it also yields insights into the raison d'etre of an autonomous element involved in a natural protein. This is of interest for the pursuit of folding mechanisms and evolutionary processes of proteins. | ||
| - | + | 10 residue folded peptide designed by segment statistics.,Honda S, Yamasaki K, Sawada Y, Morii H Structure. 2004 Aug;12(8):1507-18. PMID:15296744<ref>PMID:15296744</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 1uao" style="background-color:#fffaf0;"></div> |
| - | [[Category: Honda | + | == References == |
| - | [[Category: Yamasaki | + | <references/> |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Honda S]] | |
| - | + | [[Category: Yamasaki K]] | |
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Current revision
NMR Structure of designed protein, Chignolin, consisting of only ten amino acids (Ensembles)
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