Single protein misfolding events captured by atomic force microscopy (original) (raw)
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- Published: November 1999
Nature Structural Biology volume 6, pages 1025–1028 (1999)Cite this article
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Abstract
Using single protein atomic force microscopy (AFM) techniques we demonstrate that after repeated mechanical extension/relaxation cycles, tandem modular proteins can misfold into a structure formed by two neighboring modules. The misfolding is fully reversible and alters the mechanical topology of the modules while it is about as stable as the original fold. Our results show that modular proteins can assume a novel misfolded state and demonstrate that AFM is able to capture, in real time, rare misfolding events at the level of a single protein.
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Acknowledgements
We would like to thank H.P. Erickson (Duke University) for providing the human tenascin protein. This work was supported by NIH grants to J.M.F., P.E.M. and A.F.O.
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Authors and Affiliations
- Department of Physiology and Biophysics, Mayo Foundation, Rochester, 55905, Minnesota, USA
Andres F. Oberhauser, Piotr E. Marszalek, Mariano Carrion-Vazquez & Julio M. Fernandez
Authors
- Andres F. Oberhauser
You can also search for this author inPubMed Google Scholar - Piotr E. Marszalek
You can also search for this author inPubMed Google Scholar - Mariano Carrion-Vazquez
You can also search for this author inPubMed Google Scholar - Julio M. Fernandez
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Correspondence toJulio M. Fernandez.
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Oberhauser, A., Marszalek, P., Carrion-Vazquez, M. et al. Single protein misfolding events captured by atomic force microscopy .Nat Struct Mol Biol 6, 1025–1028 (1999). https://doi.org/10.1038/14907
- Received: 26 May 1999
- Accepted: 22 July 1999
- Issue Date: November 1999
- DOI: https://doi.org/10.1038/14907
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