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• W2133287612 endingPage "2206" @default.
• W2133287612 startingPage "2196" @default.
• W2133287612 abstract "Abstract We have examined the folding and unfolding of the caspase recruitment domain of procaspase‐1 (CP1‐CARD), a member of the α‐helical Greek key protein family. The equilibrium folding/unfolding of CP1‐CARD is described by a two‐state mechanism, and the results show CP1‐CARD is marginally stable with a Δ G of 1.1 ± 0.2 kcal/mole and an m‐value of 0.65 ± 0.06 kcal/mole/M (10 mM Tris‐HCl at pH 8.0, 1 mM DTT, 25°C). Consistent with the equilibrium folding data, CP1‐CARD is a monomer in solution when examined by size exclusion chromatography. Single‐mixing stopped‐flow refolding and unfolding studies show that CP1‐CARD folds and unfolds rapidly, with no detectable slow phases, and the reactions appear to reach equilibrium within 10 msec. However, double jump kinetic experiments demonstrate the presence of an unfolded‐like intermediate during unfolding. The intermediate converts to the fully unfolded conformation with a half‐time of 10 sec. Interrupted refolding studies demonstrate the presence of one or more nativelike intermediates during refolding, which convert to the native conformation with a half‐time of about 60 sec. Overall, the data show that both unfolding and refolding processes are slow, and the pathways contain kinetically trapped species." @default.
• W2133287612 created "2016-06-24" @default.
• W2133287612 creator A5014211882 @default.
• W2133287612 creator A5019213324 @default.
• W2133287612 date "2004-08-01" @default.
• W2133287612 modified "2023-10-17" @default.
• W2133287612 title "Kinetic traps in the folding/unfolding of procaspase‐1 CARD domain" @default.
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• W2133287612 doi "https://doi.org/10.1110/ps.03521504" @default.
• W2133287612 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2279836" @default.
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• W2133287612 hasPublicationYear "2004" @default.
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