Abstract
Atomic force microscopy (AFM) has been used in numerous studies to visualize and analyze the structure and conformation of biological samples, from single molecules to biopolymers to cells. The possibility to analyze native samples without fixation, staining and in physiological buffer conditions, combined with the sub-nanometer resolution, makes AFM a versatile tool for the analysis of protein aggregation and amyloid structures. Here, we describe the application of AFM to study fibrillar Tau protein aggregates.
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Acknowledgments
This work was supported by the Max-Planck-Society (program on “Toxic Protein Conformation,” to DM and EM), the Volkswagen Foundation (program “Conformation of Biological Molecules,” to EM), the BMBF program on Degenerative Diseases (KNDD, to EM), and the Deutsche Forschungsgemeinschaft (GK1401 at TU Dresden, to DM and SW). We are grateful to Eva-Maria Mandelkow and Subash Chinnathambi for their advice and contributions to Tau biochemistry and aggregation.
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Wegmann, S., Muller, D.J., Mandelkow, E. (2012). Investigating Fibrillar Aggregates of Tau Protein by Atomic Force Microscopy. In: Sigurdsson, E., Calero, M., Gasset, M. (eds) Amyloid Proteins. Methods in Molecular Biology, vol 849. Humana Press. https://doi.org/10.1007/978-1-61779-551-0_12
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DOI: https://doi.org/10.1007/978-1-61779-551-0_12
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