The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin
Open accessAbstract
Dynamic changes in protein conformation in response to external stimuli are important in biological processes, but it has proved difficult to directly visualize such structural changes under physiological conditions. Here, we show that high-speed atomic force microscopy can be used to visualize dynamic changes in stimulated proteins. High-resolution movies of a light-driven proton pump, bacteriorhodopsin, reveal that, upon illumination, a cytoplasmic portion of each bacteriorhodopsin monomer is brought into contact with adjacent trimers. The bacteriorhodopsin-bacteriorhodopsin interaction in the transiently formed assembly engenders both positive and negative cooperative effects in the decay kinetics as the initial bacteriorhodopsin recovers and, as a consequence, the turnover rate of the photocycle is maintained constant, on average, irrespective of the light intensity. These results confirm that high-resolution visualization is a powerful approach for studying elaborate biomolecular processes under realistic conditions.
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Cites
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Structure of bacteriorhodopsin at 1.55 Å resolution
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A high-speed atomic force microscope for studying biological macromolecules
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Self-citationImaging Crystals, Polymers, and Processes in Water with the Atomic Force Microscope
Drake, B., Prater, C. B., Weisenhorn, A. L., Gould, S. A. C., Albrecht, T. R., Quate, C. F., Cannell, D. S., Hansma, H. G., & Hansma, P. K. (1989) · Science · doi:10.1126/science.2928794 · Cited by 1,033
CLOSING IN ON BACTERIORHODOPSIN: Progress in Understanding the Molecule
Haupts, U., Tittor, J., & Oesterhelt, D. (1999) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.28.1.367 · Cited by 577
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High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes
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Self-citationStructural Changes in Bacteriorhodopsin During Ion Transport at 2 Angstrom Resolution
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Surface of bacteriorhodopsin revealed by high-resolution electron crystallography
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Cited by
Applications of biosensing atomic force microscopy in monitoring drug and nanoparticle delivery
Lamprecht, C., Hinterdorfer, P., & Ebner, A. (2014) · Expert Opinion on Drug Delivery · doi:10.1517/17425247.2014.917078 · Cited by 46
Metadata
- Authors
- Shibata, M., Yamashita, H., Uchihashi, T., Kandori, H., & Ando, T.
- Venue
- Nature Nanotechnology
- Published
- 2010-02-14
- Volume
- 5
- Issue
- 3
- Pages
- 208-212
- ISSN
- 1748-3387 (ISSN-L)
- 1748-3395
- OpenAlex
- W2062115875
- Cited by
- 320
- References
- 20
- FWCI
- 18.44
- Type
- journal article
- Language
- en
- Open access
- green
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