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| | ==NMR solution structure of Kx5Q ProtL mutant== | | ==NMR solution structure of Kx5Q ProtL mutant== |
| - | <StructureSection load='2jzp' size='340' side='right'caption='[[2jzp]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2jzp' size='340' side='right'caption='[[2jzp]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jzp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplococcus_magnus"_prevot_1933 "diplococcus magnus" prevot 1933]. 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://proteopedia.org/fgij/fg.htm?mol=2JZP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jzp]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2JZP FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2jzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jzp OCA], [http://pdbe.org/2jzp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jzp RCSB], [http://www.ebi.ac.uk/pdbsum/2jzp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jzp ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jzp OCA], [https://pdbe.org/2jzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jzp RCSB], [https://www.ebi.ac.uk/pdbsum/2jzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jzp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q51912_FINMA Q51912_FINMA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Diplococcus magnus prevot 1933]] | + | [[Category: Finegoldia magna]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aguilar-Galindo, O Millet]]
| + | [[Category: Castano D]] |
| - | [[Category: Castano, D]] | + | [[Category: Lopez-Mendez N]] |
| - | [[Category: Lopez-Mendez, N]] | + | [[Category: Millet Aguilar-Galindo O]] |
| - | [[Category: Pons, M]] | + | [[Category: Pons M]] |
| - | [[Category: Tadeo, X]] | + | [[Category: Tadeo X]] |
| - | [[Category: Cell wall]] | + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Peptidoglycan-anchor]]
| + | |
| - | [[Category: Protein]]
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| Structural highlights
Function
Q51912_FINMA
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 PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tadeo X, Lopez-Mendez B, Castano D, Trigueros T, Millet O. Protein stabilization and the Hofmeister effect: the role of hydrophobic solvation. Biophys J. 2009 Nov 4;97(9):2595-603. PMID:19883603 doi:10.1016/j.bpj.2009.08.029
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