The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Force-Clamp Spectroscopy Monitors the Folding Trajectory of a Single Protein
Abstract
We used force-clamp atomic force micoscopy to measure the end-to-end length of the small protein ubiquitin during its folding reaction at the single-molecule level. Ubiquitin was first unfolded and extended at a high force, then the stretching force was quenched and protein folding was observed. The folding trajectories were continuous and marked by several distinct stages. The time taken to fold was dependent on the contour length of the unfolded protein and the stretching force applied during folding. The folding collapse was marked by large fluctuations in the end-to-end length of the protein, but these fluctuations vanished upon the final folding contraction. These direct observations of the complete folding trajectory of a protein provide a benchmarkto determine the physical basis of the folding reaction.
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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
Heteropolymer freezing and design: Towards physical models of protein folding
Pande, V. S., Grosberg, A. Y., & Tanaka, T. (2000) · Reviews of Modern Physics · doi:10.1103/revmodphys.72.259 · Cited by 284
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Metadata
- Authors
- Fernandez, J. M., & Li, H.
- Venue
- Science
- Published
- 2004-03-12
- Volume
- 303
- Issue
- 5664
- Pages
- 1674-1678
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2090807504
- Cited by
- 536
- References
- 2
- FWCI
- 15.31
- 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.
