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- W1997788374 abstract "Protein recognition and binding play a fundamental role in living systems but sometimes also result in pathological aggregates. To probe the coupling between folding and binding in a homoheptameric system, we have characterized the time-resolved unfolding/disassembly mechanism of human co-chaperonin protein 10 (cpn10) by a combination of experimental and computational methods. The results from both approaches are in excellent agreement and make obvious that the kinetic process is three-state: an initial polypeptide-unfolding step, resulting in a non-native heptamer, is followed by a slower heptamer-dissociation step. This demonstrates that the barriers on the kinetic free-energy landscape are defined by thermodynamic stability. cpn10 is one of few, and the only heptameric, experimentally characterized system that follows the fly casting scenario of molecular recognition." @default.
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- W1997788374 date "2005-11-02" @default.
- W1997788374 modified "2023-10-15" @default.
- W1997788374 title "Unfolding of Heptameric Co-chaperonin Protein Follows “Fly Casting” Mechanism: Observation of Transient Nonnative Heptamer" @default.
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- W1997788374 doi "https://doi.org/10.1021/ja055574o" @default.
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