Identification of Distinct Soluble States During Fibril Formation Using Multilinear Analysis of NMR Diffusion Data
Jensen, Kristine Steen LU ; Nilsson, Mathias ; Akke, Mikael LU
and Malmendal, Anders
(2023)
In Methods in Molecular Biology
2551.
p.461-479
- 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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/099cf341-ede9-4759-ac27-6f3fd8d7c26c
- author
- Jensen, Kristine Steen
LU
; Nilsson, Mathias
; Akke, Mikael
LU
and Malmendal, Anders
- organization
- publishing date
- 2023
- type
- Chapter in Book/Report/Conference proceeding
- publication status
- published
- subject
- keywords
- NMR, Parallel factor analysis (PARAFAC), Protein fibrillation, Pulsed field gradient, Superoxide dismutase 1 (SOD1), Translational diffusion
- host publication
- Methods in Molecular Biology
- series title
- Methods in Molecular Biology
- editor
- Stanisław Cieplak, Andrzej
- volume
- 2551
- pages
- 19 pages
- publisher
- Humana Press
- external identifiers
-
- scopus:85141003742
- pmid:36310220
- ISSN
- 1064-3745
- 1940-6029
- ISBN
- 978-1-0716-2596-5
- 978-1-0716-2597-2
- DOI
- 10.1007/978-1-0716-2597-2_29
- language
- English
- LU publication?
- yes
- id
- 099cf341-ede9-4759-ac27-6f3fd8d7c26c
- date added to LUP
- 2023-01-24 09:02:02
- date last changed
- 2024-06-13 09:37:57
@inbook{099cf341-ede9-4759-ac27-6f3fd8d7c26c,
abstract = {{<p>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.</p>}},
author = {{Jensen, Kristine Steen and Nilsson, Mathias and Akke, Mikael and Malmendal, Anders}},
booktitle = {{Methods in Molecular Biology}},
editor = {{Stanisław Cieplak, Andrzej}},
isbn = {{978-1-0716-2596-5}},
issn = {{1064-3745}},
keywords = {{NMR; Parallel factor analysis (PARAFAC); Protein fibrillation; Pulsed field gradient; Superoxide dismutase 1 (SOD1); Translational diffusion}},
language = {{eng}},
pages = {{461--479}},
publisher = {{Humana Press}},
series = {{Methods in Molecular Biology}},
title = {{Identification of Distinct Soluble States During Fibril Formation Using Multilinear Analysis of NMR Diffusion Data}},
url = {{http://dx.doi.org/10.1007/978-1-0716-2597-2_29}},
doi = {{10.1007/978-1-0716-2597-2_29}},
volume = {{2551}},
year = {{2023}},
}