6y07

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m (Protected "6y07" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6y07 is ON HOLD
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==Designing a Granulopoietic Protein by Topological Rescaffolding 1: Sohair==
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<StructureSection load='6y07' size='340' side='right'caption='[[6y07]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6y07]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y07 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Y07 FirstGlance]. <br>
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</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=6y07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y07 OCA], [http://pdbe.org/6y07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6y07 RCSB], [http://www.ebi.ac.uk/pdbsum/6y07 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6y07 ProSAT]</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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The ability of proteins to adopt multiple conformational states is essential to their function, and elucidating the details of such diversity under physiological conditions has been a major challenge. Here we present a generalized method for mapping protein population landscapes by NMR spectroscopy. Experimental NOESY spectra are directly compared with a set of expectation spectra back-calculated across an arbitrary conformational space. Signal decomposition of the experimental spectrum then directly yields the relative populations of local conformational microstates. In this way, averaged descriptions of conformation can be eliminated. As the method quantitatively compares experimental and expectation spectra, it inherently delivers an R factor expressing how well structural models explain the input data. We demonstrate that our method extracts sufficient information from a single 3D NOESY experiment to perform initial model building, refinement, and validation, thus offering a complete de novo structure determination protocol.
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Authors: ElGamacy, M., Coles, M.
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Mapping Local Conformational Landscapes of Proteins in Solution.,ElGamacy M, Riss M, Zhu H, Truffault V, Coles M Structure. 2019 Mar 26. pii: S0969-2126(19)30083-8. doi:, 10.1016/j.str.2019.03.005. PMID:30930065<ref>PMID:30930065</ref>
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Description: Designing a Granulopoietic Protein by Topological Rescaffolding 1: Sohair
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6y07" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Coles, M]]
[[Category: Coles, M]]
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[[Category: Elgamacy, M]]
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[[Category: ElGamacy, M]]
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[[Category: De novo protein]]
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[[Category: Gcsf analog]]
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[[Category: Protein design]]
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[[Category: Receptor modulator]]

Revision as of 10:04, 18 March 2020

Designing a Granulopoietic Protein by Topological Rescaffolding 1: Sohair

PDB ID 6y07

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