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.

Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call