The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Observation of strange kinetics in protein folding
Open accessAbstract
Highly nonexponential folding kinetics in aqueous solution have been observed during temperature jump-induced refolding of two proteins, yeast phosphoglycerate kinase and a ubiquitin mutant. The observations are most easily interpreted in terms of downhill folding, which posits a heterogeneous ensemble of structures en route to the folded state. The data are also reconciled with exponential kinetics measured under different experimental conditions and with titration experiments indicating cooperative folding.
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
The Energy Landscapes and Motions of Proteins
Frauenfelder, H., Sligar, S. G., & Wolynes, P. G. (1991) · Science · doi:10.1126/science.1749933 · Cited by 3,250
Spin glasses and the statistical mechanics of protein folding.
Bryngelson, J. D., & Wolynes, P. G. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.21.7524 · Cited by 1,634
Dynamics of ligand binding to myoglobin
Austin, R. H., Beeson, K. W., Eisenstein, L., Frauenfelder, H., & Gunsalus, I. C. (1975) · Biochemistry · doi:10.1021/bi00695a021 · Cited by 1,624
Principles of protein folding — A perspective from simple exact models
Dill, K. A., Bromberg, S., Yue, K., Chan, H. S., Fiebig, K. M., Yee, D. P., & Thomas, P. D. (1995) · Protein Science · doi:10.1002/pro.5560040401 · Cited by 1,525
Theory for the folding and stability of globular proteins
Dill, K. A. (1985) · Biochemistry · doi:10.1021/bi00327a032 · Cited by 1,249
Shlesinger, M. F., Zaslavsky, G. M., & Klafter, J. (1993) · Nature · doi:10.1038/363031a0 · Cited by 1,051
The Role of Solvent Viscosity in the Dynamics of Protein Conformational Changes
Ansari, A., Jones, C. M., Henry, E. R., Hofrichter, J., & Eaton, W. A. (1992) · Science · doi:10.1126/science.1615323 · Cited by 550
Toward an outline of the topography of a realistic protein-folding funnel.
Onuchic, J. N., Wolynes, P. G., Luthey-Schulten, Z., & Socci, N. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.8.3626 · Cited by 523
Khorasanizadeh, S., Peters, I. D., & Roder, H. (1996) · Nature Structural Biology · doi:10.1038/nsb0296-193 · Cited by 346
Folding funnels and frustration in off-lattice minimalist protein landscapes
Nymeyer, H., García, A. E., & Onuchic, J. N. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.5921 · Cited by 326
Cited by
Antibody neutralization and escape by HIV-1
Wei, X., Decker, J. M., Wang, S., Hui, H., Kappes, J. C., Wu, X., Salazar-Gonzalez, J. F., Salazar, M. G., Kilby, J. M., Saag, M. S., et al. (2003) · Nature · doi:10.1038/nature01470 · Cited by 2,421
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
Folding and binding cascades: Dynamic landscapes and population shifts
Kumar, S., Ma, B., Tsai, C., Sinha, N., & Nussinov, R. (2000) · Protein Science · doi:10.1110/ps.9.1.10 · Cited by 595
Native contacts determine protein folding mechanisms in atomistic simulations
Best, R. B., Hummer, G., & Eaton, W. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311599110 · Cited by 594
Aspects of Protein Reaction Dynamics: Deviations from Simple Behavior
Karplus, M. (2000) · The Journal of Physical Chemistry B · doi:10.1021/jp993555t · Cited by 306
Metadata
- Authors
- Sabelko, J., Ervin, J., & Gruebele, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1999-05-25
- Volume
- 96
- Issue
- 11
- Pages
- 6031-6036
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2084642783
- Cited by
- 310
- References
- 24
- FWCI
- 6.42
- Type
- journal article
- Language
- en
- Open access
- green
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: Observation of strange kinetics in protein folding. https://app.cochat.ai/papers/10.1073/pnas.96.11.6031
- The paper
- Sabelko, J., Ervin, J., & Gruebele, M. (1999). Observation of strange kinetics in protein folding. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.11.6031
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.
