1ic9
From Proteopedia
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| - | [[ | + | ==NMR SOLUTION STRUCTURE OF THE DESIGNED BETA-SHEET MINI-PROTEIN TH10AOX== |
| + | <StructureSection load='1ic9' size='340' side='right' caption='[[1ic9]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1ic9]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IC9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IC9 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DPR:D-PROLINE'>DPR</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1icl|1icl]], [[1ico|1ico]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ic9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ic9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ic9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ic9 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Here we report the creation of a predominantly beta-structured mini-protein motif. The design target is based on the naturally occurring toxin hand (TH) motifs that are composed of four disulfide bonds and three loops that form a 'hand'. Analysis and subsequent modification of several generations of mini-proteins produced the final 29-residue mini-protein. The structured motif of this new mini-protein provides insight into the compensatory changes that result in the formation of a tightly packed hydrophobic core in a small, globular beta-structure motif. Additionally, this mini-motif represents a new, distinct surface topology for protein design and a valuable, yet compact, model system for the study of beta-sheet structure in water. | ||
| - | + | Design of a discretely folded mini-protein motif with predominantly beta-structure.,Ottesen JJ, Imperiali B Nat Struct Biol. 2001 Jun;8(6):535-9. PMID:11373623<ref>PMID:11373623</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Imperiali, B.]] | [[Category: Imperiali, B.]] | ||
[[Category: Ottesen, J J.]] | [[Category: Ottesen, J J.]] | ||
[[Category: De novo protein]] | [[Category: De novo protein]] | ||
[[Category: Three stranded antiparallel beta-sheet mini-protein motif de novo protein design]] | [[Category: Three stranded antiparallel beta-sheet mini-protein motif de novo protein design]] | ||
Revision as of 13:13, 28 September 2014
NMR SOLUTION STRUCTURE OF THE DESIGNED BETA-SHEET MINI-PROTEIN TH10AOX
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