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| | ==NRC consensus ankyrin repeat protein solution structure== | | ==NRC consensus ankyrin repeat protein solution structure== |
| - | <StructureSection load='2l6b' size='340' side='right'caption='[[2l6b]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2l6b' size='340' side='right'caption='[[2l6b]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2l6b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L6B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l6b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L6B 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=2l6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l6b OCA], [http://pdbe.org/2l6b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l6b RCSB], [http://www.ebi.ac.uk/pdbsum/2l6b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l6b 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=2l6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l6b OCA], [https://pdbe.org/2l6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l6b RCSB], [https://www.ebi.ac.uk/pdbsum/2l6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l6b ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aksel, T]] | + | [[Category: Aksel T]] |
| - | [[Category: Barrick, D]] | + | [[Category: Barrick D]] |
| - | [[Category: Majumdar, A]] | + | [[Category: Majumdar A]] |
| - | [[Category: Ankyrin]]
| + | |
| - | [[Category: Consensus]]
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| - | [[Category: De novo protein]]
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| - | [[Category: Ising model]]
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| - | [[Category: Nrc]]
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| - | [[Category: Repeat protein]]
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| Structural highlights
Publication Abstract from PubMed
Cooperativity is a defining feature of protein folding, but its thermodynamic and structural origins are not completely understood. By constructing consensus ankyrin repeat protein arrays that have nearly identical sequences, we quantify cooperativity by resolving stability into intrinsic and interfacial components. Heteronuclear NMR and CD spectroscopy show that these constructs adopt ankyrin repeat structures. Applying a one-dimensional Ising model to a series of constructs chosen to maximize information content in unfolding transitions, we quantify stabilities of the terminal capping repeats, and resolve the effects of denaturant into intrinsic and interfacial components. Reversible thermal denaturation resolves interfacial and intrinsic free energies into enthalpic, entropic, and heat capacity terms. Intrinsic folding is entropically disfavored, whereas interfacial interaction is entropically favored and attends a decrease in heat capacity. These results suggest that helix formation and backbone ordering occurs upon intrinsic folding, whereas hydrophobic desolvation occurs upon interfacial interaction, contributing to cooperativity.
The contribution of entropy, enthalpy, and hydrophobic desolvation to cooperativity in repeat-protein folding.,Aksel T, Majumdar A, Barrick D Structure. 2011 Mar 9;19(3):349-60. PMID:21397186[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Aksel T, Majumdar A, Barrick D. The contribution of entropy, enthalpy, and hydrophobic desolvation to cooperativity in repeat-protein folding. Structure. 2011 Mar 9;19(3):349-60. PMID:21397186 doi:10.1016/j.str.2010.12.018
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