The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding.
Open accessAbstract
How fast can a protein fold? The rate of polypeptide collapse to a compact state sets an upper limit to the rate of folding. Collapse may in turn be limited by the rate of intrachain diffusion. To address this question, we have determined the rate at which two regions of an unfolded protein are brought into contact by diffusion. Our nanosecond-resolved spectroscopy shows that under strongly denaturing conditions, regions of unfolded cytochrome separated by approximately 50 residues diffuse together in 35-40 microseconds. This result leads to an estimate of approximately (1 microsecond)-1 as the upper limit for the rate of protein folding.
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Cites
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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
From Levinthal to pathways to funnels
Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293
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
Protein folding in the landscape perspective: Chevron plots and non-arrhenius kinetics
Chan, H. S., & Dill, K. A. (1998) · Proteins: Structure, Function, and Genetics · doi:10.1002/(sici)1097-0134(19980101)30:1<2::aid-prot2>3.0.co;2-r · Cited by 438
Theoretical studies of protein-folding thermodynamics and kinetics
Shakhnovich, E. I. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80005-x · Cited by 379
Metadata
- Authors
- Hagen, S. J., Hofrichter, J., Szabo, A., & Eaton, W. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1996-10-15
- Volume
- 93
- Issue
- 21
- Pages
- 11615-11617
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1968640720
- Cited by
- 400
- References
- 27
- FWCI
- 8.53
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding. https://app.cochat.ai/papers/10.1073/pnas.93.21.11615
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- Hagen, S. J., Hofrichter, J., Szabo, A., & Eaton, W. A. (1996). Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.93.21.11615
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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.
