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Stepwise unfolding of titin under force-clamp atomic force microscopy
Open accessAbstract
Here we demonstrate the implementation of a single-molecule force clamp adapted for use with an atomic force microscope. We show that under force-clamp conditions, an engineered titin protein elongates in steps because of the unfolding of its modules and that the waiting times to unfold are exponentially distributed. Force-clamp measurements directly measure the force dependence of the unfolding probability and readily captures the different mechanical stability of the I27 and I28 modules of human cardiac titin. Force-clamp spectroscopy promises to be a direct way to probe the mechanical stability of elastic proteins such as those found in muscle, the extracellular matrix, and cell adhesion.
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Citations
Cited by
Ribas-Arino, J., & Marx, D. (2012) · Chemical Reviews · doi:10.1021/cr200399q · Cited by 448
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Alessandrini, A., & Facci, P. (2005) · Measurement Science and Technology · doi:10.1088/0957-0233/16/6/r01 · Cited by 384
Müller, D. J., Dumitru, A. C., Lo Giudice, C., Gaub, H. E., Hinterdorfer, P., Hummer, G., De Yoreo, J. J., Dufrêne, Y. F., & Alsteens, D. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00617 · Cited by 259
Hariharan, V., & Hancock, W. O. (2009) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-009-0059-5 · Cited by 82
Banwait, J. K., Islam, L., & Lucius, A. L. (2024) · eLife · doi:10.7554/elife.99052 · Cited by 6
Metadata
- Authors
- Oberhauser, A. F., Hansma, P. K., Carrion-Vazquez, M., & Fernandez, J. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2001-01-09
- Volume
- 98
- Issue
- 2
- Pages
- 468-472
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2104559182
- Cited by
- 367
- References
- 0
- FWCI
- 12.73
- Type
- journal article
- Language
- en
- Open access
- green
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- Oberhauser, A. F., Hansma, P. K., Carrion-Vazquez, M., & Fernandez, J. M. (2001). Stepwise unfolding of titin under force-clamp atomic force microscopy. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.98.2.468
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