1tuc
ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT S19-P20
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OverviewOverview
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 StructureAbout this Structure
1TUC is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
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
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