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1yzc

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[[Image:1yzc.png|left|200px]]
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==The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) with the N- and a part of the C-terminal helices unfolded==
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<StructureSection load='1yzc' size='340' side='right' caption='[[1yzc]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1yzc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YZC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YZC FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yza|1yza]]</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=1yzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yzc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yzc RCSB], [http://www.ebi.ac.uk/pdbsum/1yzc PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yz/1yzc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Using native-state hydrogen-exchange-directed protein engineering and multidimensional NMR, we determined the high-resolution structure (rms deviation, 1.1 angstroms) for an intermediate of the four-helix bundle protein: Rd-apocytochrome b562. The intermediate has the N-terminal helix and a part of the C-terminal helix unfolded. In earlier studies, we also solved the structures of two other folding intermediates for the same protein: one with the N-terminal helix alone unfolded and the other with a reorganized hydrophobic core. Together, these structures provide a description of a protein folding pathway with multiple intermediates at atomic resolution. The two general features for the intermediates are (i) native-like backbone topology and (ii) nonnative side-chain interactions. These results have implications for important issues in protein folding studies, including large-scale conformation search, -value analysis, and computer simulations.
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{{STRUCTURE_1yzc| PDB=1yzc | SCENE= }}
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A protein folding pathway with multiple folding intermediates at atomic resolution.,Feng H, Zhou Z, Bai Y Proc Natl Acad Sci U S A. 2005 Apr 5;102(14):5026-31. Epub 2005 Mar 25. PMID:15793003<ref>PMID:15793003</ref>
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===The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) with the N- and a part of the C-terminal helices unfolded===
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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_15793003}}
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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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[[1yzc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YZC OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:015793003</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: BSGC, Berkeley Structural Genomics Center.]]
[[Category: BSGC, Berkeley Structural Genomics Center.]]

Revision as of 19:09, 29 September 2014

The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) with the N- and a part of the C-terminal helices unfolded

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