The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Direct Observation of Enzyme Activity with the Atomic Force Microscope
Abstract
The height fluctuations on top of the protein lysozyme adsorbed on mica were measured locally with an atomic force microscope operated in tapping mode in liquid. Height fluctuations of an apparent size of 1 nanometer that lasted for about 50 milliseconds were observed over lysozyme molecules when a substrate (oligoglycoside) was present. In the presence of the inhibitor chitobiose, these height fluctuations decreased to the level without the oligoglycoside. The most straightforward interpretation of these results is that the height fluctuations correspond to the conformational changes of lysozyme during hydrolysis. It is also possible, however, that the height fluctuations are, at least in part, the result of a different height or elasticity of the transient complex of lysozyme plus the substrate.
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Citations
Cites
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
Cited by
Protein adsorption on solid surfaces
Hlady, V., & Buijs, J. (1996) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(96)80098-x · Cited by 522
Mechanical Stability of Single DNA Molecules
Clausen-Schaumann, H., Rief, M., Tolksdorf, C., & Gaub, H. E. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76747-6 · Cited by 437
Rotsch, C., Jacobson, K., & Radmacher, M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.3.921 · Cited by 437
Self-citationNative Escherichia coli OmpF Porin Surfaces Probed by Atomic Force Microscopy
Schabert, F. A., Henn, C., & Engel, A. (1995) · Science · doi:10.1126/science.7701347 · Cited by 279
Tapping-Mode Atomic Force Microscopy Produces Faithful High-Resolution Images of Protein Surfaces
Möller, C., Allen, M., Elings, V., Engel, A., & Müller, D. J. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)76966-3 · Cited by 274
Metadata
- Authors
- Radmacher, M., Fritz, M., Hansma, H. G., & Hansma, P. K.
- Venue
- Science
- Published
- 1994-09-09
- Volume
- 265
- Issue
- 5178
- Pages
- 1577-1579
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2072306011
- Cited by
- 405
- References
- 1
- FWCI
- 26.86
- Type
- journal article
- Language
- en
- Open access
- closed
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- Radmacher, M., Fritz, M., Hansma, H. G., & Hansma, P. K. (1994). Direct Observation of Enzyme Activity with the Atomic Force Microscope. Science. https://doi.org/10.1126/science.8079171
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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.
