The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Optical Trapping of a Single Protein
Abstract
We experimentally demonstrate the optical trapping of a single bovine serum albumin (BSA) molecule that has a hydrodynamic radius of 3.4 nm, using a double-nanohole in an Au film. The strong optical force in the trap not only stably traps the protein molecule but also unfolds it. The unfolding of the BSA is confirmed by experiments with changing optical power and with changing solution pH. The detection of the trapping event has a signal-to-noise ratio of 33, which shows that the setup is extremely sensitive to detect the presence of a protein, even at the single molecule level.
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Citations
Cites
Observation of a single-beam gradient force optical trap for dielectric particles
Ashkin, A., Dziedzic, J. M., Bjorkholm, J. E., & Chu, S. (1986) · Optics Letters · doi:10.1364/ol.11.000288 · Cited by 7,030
Biosensing with plasmonic nanosensors
Anker, J. N., Hall, W. P., Lyandres, O., Shah, N. C., Zhao, J., & Van Duyne, R. P. (2008) · Nature Materials · doi:10.1038/nmat2162 · Cited by 6,786
Carter, D. C., & Ho, J. X. (1994) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60640-3 · Cited by 3,187
Optical Trapping and Manipulation of Viruses and Bacteria
Ashkin, A., & Dziedzic, J. M. (1987) · Science · doi:10.1126/science.3547653 · Cited by 2,191
Single myosin molecule mechanics: piconewton forces and nanometre steps
Finer, J. T., Simmons, R. M., & Spudich, J. A. (1994) · Nature · doi:10.1038/368113a0 · Cited by 1,915
Whispering-gallery-mode biosensing: label-free detection down to single molecules
Vollmer, F., & Arnold, S. (2008) · Nature Methods · doi:10.1038/nmeth.1221 · Cited by 1,660
Stretching DNA with optical tweezers
Wang, M. D., Yin, H., Landick, R., Gelles, J., & Block, S. M. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78780-0 · Cited by 1,481
Direct observation of base-pair stepping by RNA polymerase
Abbondanzieri, E. A., Greenleaf, W. J., Shaevitz, J. W., Landick, R., & Block, S. M. (2005) · Nature · doi:10.1038/nature04268 · Cited by 855
Immunosensors—principles and applications to clinical chemistry
Luppa, P. B., Sokoll, L. J., & Chan, D. W. (2001) · Clinica Chimica Acta · doi:10.1016/s0009-8981(01)00629-5 · Cited by 741
Ostuni, E., Chapman, R. G., Liang, M. N., Meluleni, G., Pier, G., Ingber, D. E., & Whitesides, G. M. (2001) · Langmuir · doi:10.1021/la010552a · Cited by 563
Cited by
From molecular to supramolecular electronics
Chen, H., & Fraser Stoddart, J. (2021) · Nature Reviews Materials · doi:10.1038/s41578-021-00302-2 · Cited by 380
Yoo, D., Gurunatha, K. L., Choi, H.-K., Mohr, D. A., Ertsgaard, C. T., Gordon, R., & Oh, S.-H. (2018) · Nano Letters · doi:10.1021/acs.nanolett.8b00732 · Cited by 173
Self-citationOptical Monitoring of In Situ Iron Loading into Single, Native Ferritin Proteins
Yousefi, A., Ying, C., Parmenter, C. D. J., Assadipapari, M., Sanderson, G., Zheng, Z., Xu, L., Zargarbashi, S., Hickman, G. J., Cousins, R. B., et al. (2023) · Nano Letters · doi:10.1021/acs.nanolett.3c00042 · Cited by 37
Metadata
- Authors
- Pang, Y., & Gordon, R.
- Venue
- Nano Letters
- Publisher
- American Chemical Society (ACS)
- Published
- 2011-12-16
- Volume
- 12
- Issue
- 1
- Pages
- 402-406
- ISSN
- 1530-6984 (ISSN-L)
- 1530-6992
- OpenAlex
- W2073614756
- Cited by
- 503
- References
- 26
- FWCI
- 12.51
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
