The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Unfolding Pathways of Individual Bacteriorhodopsins
Abstract
Atomic force microscopy and single-molecule force spectroscopy were combined to image and manipulate purple membrane patches from Halobacterium salinarum . Individual bacteriorhodopsin molecules were first localized and then extracted from the membrane; the remaining vacancies were imaged again. Anchoring forces between 100 and 200 piconewtons for the different helices were found. Upon extraction, the helices were found to unfold. The force spectra revealed the individuality of the unfolding pathways. Helices G and F as well as helices E and D always unfolded pairwise, whereas helices B and C occasionally unfolded one after the other. Experiments with cleaved loops revealed the origin of the individuality: stabilization of helix B by neighboring helices.
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Self-citationMEMBRANE PROTEIN FOLDING AND STABILITY: Physical Principles
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Self-citationStructure of bacteriorhodopsin at 1.55 Å resolution
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Metadata
- Authors
- Oesterhelt, F., Oesterhelt, D., Pfeiffer, M., Engel, A., Gaub, H. E., & Müller, D. J.
- Venue
- Science
- Published
- 2000-04-07
- Volume
- 288
- Issue
- 5463
- Pages
- 143-146
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1993114893
- Cited by
- 686
- References
- 44
- FWCI
- 26.55
- Type
- journal article
- Language
- en
- Open access
- closed
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- Oesterhelt, F., Oesterhelt, D., Pfeiffer, M., Engel, A., Gaub, H. E., & Müller, D. J. (2000). Unfolding Pathways of Individual Bacteriorhodopsins. Science. https://doi.org/10.1126/science.288.5463.143
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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.
