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Fluorescence quenching: A tool for single-molecule protein-folding study
Open accessAbstract
By using titin as a model system, we have demonstrated that fluorescence quenching can be used to study protein folding at the single molecule level. The unfolded titin molecules with multiple dye molecules attached are able to fold to the native state. In the native folded state, the fluorescence from dye molecules is quenched due to the close proximity between the dye molecules. Unfolding of the titin leads to a dramatic increase in the fluorescence intensity. Such a change makes the folded and unfolded states of a single titin molecule clearly distinguishable and allows us to measure the folding dynamics of individual titin molecules in real time. We have also shown that fluorescence quenching can signal folding and unfolding of a small protein with only one immunoglobulin domain.
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Cites
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
THEORY OF PROTEIN FOLDING: The Energy Landscape Perspective
Onuchic, J. N., Luthey-Schulten, Z., & Wolynes, P. G. (1997) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.48.1.545 · Cited by 2,210
Cited by
Zhao, G.-J., & Han, K.-L. (2007) · The Journal of Physical Chemistry A · doi:10.1021/jp068420j · Cited by 622
Force-Induced Unfolding of Fibronectin in the Extracellular Matrix of Living Cells
Smith, M. L., Gourdon, D., Little, W. C., Kubow, K. E., Eguiluz, R. A., Luna-Morris, S., & Vogel, V. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050268 · Cited by 440
Zhao, G.-J., & Han, K.-L. (2007) · The Journal of Physical Chemistry A · doi:10.1021/jp0719659 · Cited by 414
The protein import motor of mitochondria
Neupert, W., & Brunner, M. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm878 · Cited by 393
Photophysical processes in single molecule organic fluorescent probes
Stennett, E. M. S., Ciuba, M. A., & Levitus, M. (2014) · Chem. Soc. Rev. · doi:10.1039/c3cs60211g · Cited by 323
Metadata
- Authors
- Zhuang, X., Ha, T., Kim, H. D., Centner, T., Labeit, S., & Chu, S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-12-19
- Volume
- 97
- Issue
- 26
- Pages
- 14241-14244
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2029349765
- Cited by
- 196
- References
- 2
- FWCI
- 3.27
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Zhuang, X., Ha, T., Kim, H. D., Centner, T., Labeit, S., & Chu, S. (2000). Fluorescence quenching: A tool for single-molecule protein-folding study. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.97.26.14241
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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.
