2jzp

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[[Image:2jzp.png|left|200px]]
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==NMR solution structure of Kx5Q ProtL mutant==
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<StructureSection load='2jzp' size='340' side='right' caption='[[2jzp]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2jzp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JZP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JZP FirstGlance]. <br>
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</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=2jzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jzp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jzp RCSB], [http://www.ebi.ac.uk/pdbsum/2jzp 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/jz/2jzp_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 the IGg binding domain of protein L from Streptoccocal magnus (ProtL) as a case study, we investigated how the anions of the Hofmeister series affect protein stability. To that end, a suite of lysine-to-glutamine modifications were obtained and structurally and thermodynamically characterized. The changes in stability introduced with the mutation are related to the solvent-accessible area of the side chain, specifically to the solvation of the nonpolar moiety of the residue. The thermostability for the set of ProtL mutants was determined in the presence of varying concentrations (0-1 M) of six sodium salts from the Hofmeister series: sulfate, phosphate, fluoride, nitrate, perchlorate, and thiocyanate. For kosmotropic anions (sulfate, phosphate, and fluoride), the stability changes induced by the cosolute (encoded in m(3)=deltaDeltaG(0)/deltaC(3)) are proportional to the surface changes introduced with the mutation. In contrast, the m(3) values measured for chaotropic anions are much more independent of such surface modifications. Our results are consistent with a model in which the increase in the solution surface tension induced by the anion stabilizes the folded conformation of the protein. This contribution complements the nonspecific and weak interactions between the ions and the protein backbone that shift the equilibrium toward the unfolded state.
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{{STRUCTURE_2jzp| PDB=2jzp | SCENE= }}
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Protein stabilization and the Hofmeister effect: the role of hydrophobic solvation.,Tadeo X, Lopez-Mendez B, Castano D, Trigueros T, Millet O Biophys J. 2009 Nov 4;97(9):2595-603. PMID:19883603<ref>PMID:19883603</ref>
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===NMR solution structure of Kx5Q ProtL mutant===
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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_19883603}}
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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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[[2jzp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JZP OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:019883603</ref><references group="xtra"/>
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[[Category: Finegoldia magna]]
[[Category: Finegoldia magna]]
[[Category: Aguilar-Galindo, O Millet.]]
[[Category: Aguilar-Galindo, O Millet.]]

Revision as of 10:54, 30 September 2014

NMR solution structure of Kx5Q ProtL mutant

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