The DOI matches its Crossref record; 112 of the 112 references it cites were found in a registry or an index.
High-Resolution, Single-Molecule Measurements of Biomolecular Motion
Open accessAbstract
Many biologically important macromolecules undergo motions that are essential to their function. Biophysical techniques can now resolve the motions of single molecules down to the nanometer scale or even below, providing new insights into the mechanisms that drive molecular movements. This review outlines the principal approaches that have been used for high-resolution measurements of single-molecule motion, including centroid tracking, fluorescence resonance energy transfer, magnetic tweezers, atomic force microscopy, and optical traps. For each technique, the principles of operation are outlined, the capabilities and typical applications are examined, and various practical issues for implementation are considered. Extensions to these methods are also discussed, with an eye toward future application to outstanding biological problems.
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Cites
Reversible Unfolding of Individual Titin Immunoglobulin Domains by AFM
Rief, M., Gautel, M., Oesterhelt, F., Fernandez, J. M., & Gaub, H. E. (1997) · Science · doi:10.1126/science.276.5315.1109 · Cited by 3,077
Smith, S. B., Cui, Y., & Bustamante, C. (1996) · Science · doi:10.1126/science.271.5250.795 · Cited by 2,770
Dynamic strength of molecular adhesion bonds
Evans, E., & Ritchie, K. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78802-7 · Cited by 2,549
Direct observation of the rotation of F1-ATPase
Noji, H., Yasuda, R., Yoshida, M., & Kinosita, K. (1997) · Nature · doi:10.1038/386299a0 · Cited by 2,236
Neuman, K. C., & Block, S. M. (2004) · Review of Scientific Instruments · doi:10.1063/1.1785844 · Cited by 2,165
Self-citationSingle 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
Direct observation of kinesin stepping by optical trapping interferometry
Svoboda, K., Schmidt, C. F., Schnapp, B. J., & Block, S. M. (1993) · Nature · doi:10.1038/365721a0 · Cited by 1,910
Self-citationMyosin V Walks Hand-Over-Hand: Single Fluorophore Imaging with 1.5-nm Localization
Yildiz, A., Forkey, J. N., McKinney, S. A., Ha, T., Goldman, Y. E., & Selvin, P. R. (2003) · Science · doi:10.1126/science.1084398 · Cited by 1,837
Direct Mechanical Measurements of the Elasticity of Single DNA Molecules by Using Magnetic Beads
Smith, S. B., Finzi, L., & Bustamante, C. (1992) · Science · doi:10.1126/science.1439819 · Cited by 1,817
Biological Applications of Optical Forces
Svoboda, K., & Block, S. M. (1994) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.bb.23.060194.001335 · Cited by 1,792
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Höfling, F., & Franosch, T. (2013) · Reports on Progress in Physics · doi:10.1088/0034-4885/76/4/046602 · Cited by 1,247
Recent Advances in Optical Tweezers
Moffitt, J. R., Chemla, Y. R., Smith, S. B., & Bustamante, C. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.043007.090225 · Cited by 1,084
Ribas-Arino, J., & Marx, D. (2012) · Chemical Reviews · doi:10.1021/cr200399q · Cited by 448
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Brunger, A. T., Weninger, K., Bowen, M., & Chu, S. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.070306.103621 · Cited by 107
Metadata
- Authors
- Greenleaf, W. J., Woodside, M. T., & Block, S. M.
- Venue
- Annual Review of Biophysics and Biomolecular Structure
- Publisher
- Annual Reviews
- Published
- 2007-06-01
- Volume
- 36
- Issue
- 1
- Pages
- 171-190
- ISSN
- 1056-8700 (ISSN-L)
- 1545-4266
- OpenAlex
- W2114229182
- Cited by
- 462
- References
- 112
- FWCI
- 21.41
- Type
- journal article
- Language
- en
- Open access
- green
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- Greenleaf, W. J., Woodside, M. T., & Block, S. M. (2007). High-Resolution, Single-Molecule Measurements of Biomolecular Motion. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.biophys.36.101106.101451
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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.