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Identification of Distinct Soluble States During Fibril Formation Using Multilinear Analysis of NMR Diffusion Data
Kristine Steen Jensen1, Mathias Nilsson2, Mikael Akke3
1Biophysical Chemistry, Center for Molecular Protein Science, Department of Chemistry, Lund University, Lund, Sweden. kristine.steen_jensen@bpc.lu.se.
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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