Abstract
Protein misfolding and self-assembling into amyloid structures are associated with a number of diseases. Characterization of protein amyloid formation reactions is a challenging task as transient populations of multiple species are involved. Here we outline a method for identification and characterization of the individual soluble states during protein amyloid formation. The method combines NMR translational diffusion measurements with multilinear data analysis.
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Acknowledgment
We thank Ulrich Weininger for his help with the HSQC-based DOSY experiments.
The work founding this protocol is supported by the Swedish Research Council (2014-5815 to M.A) and (2020-04888 to KSJ), the Danish Council for Independent Research, Sapere Aude: DFF Research Talent (DFF − 4002-00258 to KSJ), and the Engineering and Physical Sciences Research Council (EP/E05899X/1 to MN).
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Jensen, K.S., Nilsson, M., Akke, M., Malmendal, A. (2023). Identification of Distinct Soluble States During Fibril Formation Using Multilinear Analysis of NMR Diffusion Data. In: Cieplak, A.S. (eds) Protein Aggregation. Methods in Molecular Biology, vol 2551. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2597-2_29
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DOI: https://doi.org/10.1007/978-1-0716-2597-2_29
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