ArticleProtein science : a publication of the Protein Society2004
Kinetic traps in the folding/unfolding of procaspase-1 CARD domain.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Assembly and regulation of ASC specks.Cellular and molecular life sciences : CMLS · 2017Review
- Structure and assembly of the mouse ASC inflammasome by combined NMR spectroscopy and cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structural mechanisms in NLR inflammasome signaling.Current opinion in structural biology · 2014Review
- Ubiquitin regulates caspase recruitment domain-mediated signaling by nucleotide-binding oligomerization domain-containing proteins NOD1 and NOD2.The Journal of biological chemistry · 2013Article
- Folding of an all-helical Greek-key protein monitored by quenched-flow hydrogen-deuterium exchange and NMR spectroscopy.European biophysics journal : EBJ · 2012Article
- Article
- Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-beta stability, oligomerization, and aggregation: amyloid-beta destabilization promotes annular protofibril formation.The Journal of biological chemistry · 2011Article
- Topology is the principal determinant in the folding of a complex all-alpha Greek key death domain from human FADD.Journal of molecular biology · 2009Article
- Protein folding: then and now.Archives of biochemistry and biophysics · 2008Article
- Rapid folding and unfolding of Apaf-1 CARD.Journal of molecular biology · 2007Article
- Substitutions of prolines examine their role in kinetic trap formation of the caspase recruitment domain (CARD) of RICK.Protein science : a publication of the Protein Society · 2006Article
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2 authors.
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Abstract
We have examined the folding and unfolding of the caspase recruitment domain of procaspase-1 (CP1-CARD), a member of the alpha-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 DeltaG(H2O) 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 degrees 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.
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