1tuc
From Proteopedia
(New page: 200px<br /><applet load="1tuc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tuc, resolution 2.02Å" /> '''ALPHA-SPECTRIN SRC H...) |
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| - | [[Image:1tuc.gif|left|200px]]<br /><applet load="1tuc" size=" | + | [[Image:1tuc.gif|left|200px]]<br /><applet load="1tuc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tuc, resolution 2.02Å" /> | caption="1tuc, resolution 2.02Å" /> | ||
'''ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT S19-P20'''<br /> | '''ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT S19-P20'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have analyzed the structure, stability and folding kinetics of | + | We have analyzed the structure, stability and folding kinetics of circularly permuted forms of alpha-spectrin SH3 domain. All the possible permutations involving the disruption of the covalent linkage between two beta-strands forming a beta-hairpin have been done. The different proteins constructed here fold to a native conformation similar to that of wild-type protein, as demonstrated by nuclear magnetic resonance and circular dichroism. Although all the mutants have similar stabilities (they are 1 to 2 kcal mol-1 less stable than the wild-type) their rate constants for folding and unfolding are quite different. Protein engineering, in combination with kinetics indicates that the folding pathway has been changed in the circularly permuted proteins. We conclude that neither the order of secondary structure elements, nor the preservation of any of the beta-hairpins present in this domain, is crucial for the ability of the polypeptide to fold, but they influence the folding and unfolding kinetics and could determine its folding pathway. |
==About this Structure== | ==About this Structure== | ||
| - | 1TUC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http:// | + | 1TUC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Serrano, L.]] | [[Category: Serrano, L.]] | ||
| - | [[Category: Viguera, A | + | [[Category: Viguera, A R.]] |
[[Category: Wilmanns, M.]] | [[Category: Wilmanns, M.]] | ||
[[Category: calcium-binding]] | [[Category: calcium-binding]] | ||
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[[Category: sh3 domain]] | [[Category: sh3 domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:25 2008'' |
Revision as of 13:17, 21 February 2008
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ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT S19-P20
Overview
We have analyzed the structure, stability and folding kinetics of circularly permuted forms of alpha-spectrin SH3 domain. All the possible permutations involving the disruption of the covalent linkage between two beta-strands forming a beta-hairpin have been done. The different proteins constructed here fold to a native conformation similar to that of wild-type protein, as demonstrated by nuclear magnetic resonance and circular dichroism. Although all the mutants have similar stabilities (they are 1 to 2 kcal mol-1 less stable than the wild-type) their rate constants for folding and unfolding are quite different. Protein engineering, in combination with kinetics indicates that the folding pathway has been changed in the circularly permuted proteins. We conclude that neither the order of secondary structure elements, nor the preservation of any of the beta-hairpins present in this domain, is crucial for the ability of the polypeptide to fold, but they influence the folding and unfolding kinetics and could determine its folding pathway.
About this Structure
1TUC is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics., Viguera AR, Blanco FJ, Serrano L, J Mol Biol. 1995 Apr 7;247(4):670-81. PMID:7723022
Page seeded by OCA on Thu Feb 21 15:17:25 2008
