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1k09

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[[Image:1k09.png|left|200px]]
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==Solution structure of BetaCore, A Designed Water Soluble Four-Stranded Antiparallel b-sheet Protein==
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<StructureSection load='1k09' size='340' side='right' caption='[[1k09]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1k09]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K09 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K09 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=CLG:2-AMINO-6-[2-(2-AMINOOXY-ACETYLAMINO)-ACETYLAMINO]-HEXANOIC+ACID'>CLG</scene>, <scene name='pdbligand=CLH:2-AMINO-6-[2-(2-OXO-ACETYLAMINO)-ACETYLAMINO]-HEXANOIC+ACID'>CLH</scene>, <scene name='pdbligand=MPT:BETA-MERCAPTOPROPIONIC+ACID'>MPT</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<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=1k09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k09 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1k09 RCSB], [http://www.ebi.ac.uk/pdbsum/1k09 PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BetaCore is a designed approximately 50-residue protein in which two BPTI-derived core modules, CM I and CM II, are connected by a 22-atom cross-link. At low temperature and pH 3, homo- and heteronuclear NMR data report a dominant folded ('f') conformation with well-dispersed chemical shifts, i, i+1 periodicity, numerous long-range NOEs, and slowed amide hydrogen isotope exchange patterns that is a four-stranded antiparallel beta-sheet with nonsymmetrical and specific association of CM I and CM II. BetaCore 'f' conformations undergo reversible, global, moderately cooperative, non-two-state thermal transitions to an equilibrium ensemble of unfolded 'u' conformations. There is a significant energy barrier between 'f' and 'u' conformations. This is the first designed four-stranded antiparallel beta-sheet that folds in water.
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{{STRUCTURE_1k09| PDB=1k09 | SCENE= }}
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BetaCore, a designed water soluble four-stranded antiparallel beta-sheet protein.,Carulla N, Woodward C, Barany G Protein Sci. 2002 Jun;11(6):1539-51. PMID:12021452<ref>PMID:12021452</ref>
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===Solution structure of BetaCore, A Designed Water Soluble Four-Stranded Antiparallel b-sheet Protein===
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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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{{ABSTRACT_PUBMED_12021452}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1k09]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K09 OCA].
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</StructureSection>
[[Category: Barany, G.]]
[[Category: Barany, G.]]
[[Category: Carulla, N.]]
[[Category: Carulla, N.]]

Revision as of 10:23, 28 September 2014

Solution structure of BetaCore, A Designed Water Soluble Four-Stranded Antiparallel b-sheet Protein

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