Identification of Distinct Soluble States During Fibril Formation Using Multilinear Analysis of NMR Diffusion Data

Kristine Steen Jensen, Mathias Nilsson, Mikael Akke, Anders Malmendal

Research output: Chapter in Book/Report/Conference proceedingBook chapterResearchpeer-review

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.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
EditorsAndrzej Stanisław Cieplak
PublisherHumana Press
Pages461-479
Number of pages19
ISBN (Electronic)978-1-0716-2597-2
ISBN (Print)978-1-0716-2596-5
DOIs
Publication statusPublished - 2023

Publication series

NameMethods in Molecular Biology
Volume2551
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

Subject classification (UKÄ)

  • Biophysics

Free keywords

  • NMR
  • Parallel factor analysis (PARAFAC)
  • Protein fibrillation
  • Pulsed field gradient
  • Superoxide dismutase 1 (SOD1)
  • Translational diffusion

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