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Cited by 316

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Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation

Open access
Mayor, Ugo, Johnson, Christopher M., Daggett, Valerie, Fersht, Alan R.·2000·Proceedings of the National Academy of Sciences

Abstract

The Engrailed Homeodomain protein has the highest refolding and unfolding rate constants directly observed to date. Temperature jump relaxation measurements gave a refolding rate constant of 37,500 s −1 in water at 25°C, rising to 51,000 s −1 around 42°C. The unfolding rate constant was 1,100 s −1 in water at 25°C and 205,000 s −1 at 63°C. The unfolding half-life is extrapolated to be ≈7.5 ns at 100°C, which allows real-time molecular dynamics unfolding simulations to be tested on this system at a realistic temperature. Preliminary simulations did indeed conform to unfolding on this time scale. Further, similar transition states were observed in simulations at 100°C and 225°C, suggesting that high-temperature simulations provide results applicable to lower temperatures.

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Crossref · 10.1073/pnas.250473497

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Metadata

Authors
Mayor, U., Johnson, C. M., Daggett, V., & Fersht, A. R.
Venue
Proceedings of the National Academy of Sciences
Published
2000-11-21
Volume
97
Issue
25
Pages
13518-13522
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2088780328
Cited by
316
References
1
FWCI
7.21
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. https://app.cochat.ai/papers/10.1073/pnas.250473497
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Mayor, U., Johnson, C. M., Daggett, V., & Fersht, A. R. (2000). Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.250473497

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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