The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Smaller and Faster: The 20-Residue Trp-Cage Protein Folds in 4 μs
Abstract
We have used laser temperature jump spectroscopy to measure the folding speed of the 20-residue Trp-cage, the smallest polypeptide known to exhibit truly cooperative folding behavior. The observed folding time (4 mus at room temperature) makes this not only the smallest foldable protein, but also the fastest, with a folding speed that exceeds contact-order predictions and approaches anticipated diffusional "speed limits" for protein folding.
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Citations
Cites
Designing a 20-residue protein
Neidigh, J. W., Fesinmeyer, R. M., & Andersen, N. H. (2002) · Nature Structural Biology · doi:10.1038/nsb798 · Cited by 793
Cited by
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
Trp-cage: Folding free energy landscape in explicit water
Zhou, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2233312100 · Cited by 363
Protein oligomerization: How and why
Ali, M. H., & Imperiali, B. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.05.037 · Cited by 356
Understanding folding and design: Replica-exchange simulations of ``Trp-cage'' miniproteins
Pitera, J. W., & Swope, W. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1330954100 · Cited by 344
Sub-microsecond Protein Folding
Kubelka, J., Chiu, T. K., Davies, D. R., Eaton, W. A., & Hofrichter, J. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.03.034 · Cited by 255
Metadata
- Authors
- Qiu, L., Pabit, S. A., Roitberg, A. E., & Hagen, S. J.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-10-12
- Volume
- 124
- Issue
- 44
- Pages
- 12952-12953
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W1990606222
- Cited by
- 333
- References
- 1
- FWCI
- 5.40
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
