2jzz: Difference between revisions
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==Solid-State NMR Structure of Microcrystalline Ubiquitin== | ==Solid-State NMR Structure of Microcrystalline Ubiquitin== | ||
<StructureSection load='2jzz' size='340' side='right' caption='[[2jzz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2jzz' size='340' side='right' caption='[[2jzz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jzz]] 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=2JZZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JZZ FirstGlance]. <br> | <table><tr><td colspan='2'>[[2jzz]] 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=2JZZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JZZ FirstGlance]. <br> | ||
</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=2jzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jzz OCA], [http://pdbe.org/2jzz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jzz RCSB], [http://www.ebi.ac.uk/pdbsum/2jzz PDBsum]</span></td></tr> | </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=2jzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jzz OCA], [http://pdbe.org/2jzz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jzz RCSB], [http://www.ebi.ac.uk/pdbsum/2jzz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jzz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/2jzz_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/2jzz_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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[[Category: Manolikas, T]] | [[Category: Manolikas, T]] | ||
[[Category: Meier, B H]] | [[Category: Meier, B H]] | ||
[[Category: Cytoplasm]] | |||
[[Category: Protein microcrystal]] | [[Category: Protein microcrystal]] | ||
[[Category: Signaling protein]] | [[Category: Signaling protein]] | ||
[[Category: Ubl conjugation]] | |||
Revision as of 13:15, 18 July 2018
Solid-State NMR Structure of Microcrystalline UbiquitinSolid-State NMR Structure of Microcrystalline Ubiquitin
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProton-driven 13C spin diffusion (PDSD) is a simple and robust two-dimensional NMR experiment. It leads to spectra with a high signal-to-noise ratio in which cross-peaks contain information about internuclear distances. We show that the total information content is sufficient to determine the atomic-resolution structure of a small protein from a single, uniformly 13C-, 15N-labeled microcrystalline sample. For the example of ubiquitin, the structure was determined by a manual procedure followed by an automatic optimization of the manual structure as well as by a fully automated structure determination approach. The relationship between internuclear distances and cross-peak intensities in the spectra is investigated. Protein structure determination from 13C spin-diffusion solid-state NMR spectroscopy.,Manolikas T, Herrmann T, Meier BH J Am Chem Soc. 2008 Mar 26;130(12):3959-66. Epub 2008 Mar 6. PMID:18321098[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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