The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation
Open accessAbstract
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Cited by
Monitoring Drug Target Engagement in Cells and Tissues Using the Cellular Thermal Shift Assay
Molina, D. M., Jafari, R., Ignatushchenko, M., Seki, T., Larsson, E. A., Dan, C., Sreekumar, L., Cao, Y., & Nordlund, P. (2013) · Science · doi:10.1126/science.1233606 · Cited by 2,261
The protein folding ‘speed limit’
Kubelka, J., Hofrichter, J., & Eaton, W. A. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.01.013 · Cited by 830
The complete folding pathway of a protein from nanoseconds to microseconds
Mayor, U., Guydosh, N. R., Johnson, C. M., Grossmann, J. G., Sato, S., Jas, G. S., Freund, S. M. V., Alonso, D. O. V., Daggett, V., & Fersht, A. R. (2003) · Nature · doi:10.1038/nature01428 · Cited by 458
Self-citationIs there a unifying mechanism for protein folding?
Daggett, V., & Fersht, A. R. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)00012-9 · Cited by 454
Self-citationFolding a protein in a computer: An atomic description of the folding/unfolding of protein A
García, A. E., & Onuchic, J. N. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2335541100 · Cited by 333
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- 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
- The paper
- 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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.