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Dissociation from the Oligomeric State Is the Rate-limiting Step in Fibril Formation by K-Casein

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Date

2008

Authors

Ecroyd, Heath
Koudelka, Tomas
Thorn, Davic C.
Williams, Danielle M.
Devlin, Glyn
Hoffmann, Peter
Carver, John

Journal Title

Journal ISSN

Volume Title

Publisher

American Society for Biochemistry and Molecular Biology Inc

Abstract

Amyloid fibrils are aggregated and precipitated forms of protein in which the protein exists in highly ordered, long, unbranching threadlike formations that are stable and resistant to degradation by proteases. Fibril formation is an ordered process that

Description

Keywords

Keywords: Agglomeration; Casein; Dissociation; Glycoproteins; High performance liquid chromatography; Mass spectrometry; Nucleation; Self assembled monolayers; Steelmaking; Turbidity; Aggregation mechanisms; Amyloid fibrils; Fibril formations; Fluorescence intensit

Citation

URI

http://hdl.handle.net/1885/63151

Collections

Open Access Research

Source

Journal of Biological Chemistry

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

10.1074/jbc.M709928200

Restricted until

2037-12-31

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Description
01_Ecroyd_Dissociation_from_the_2008.pdf (1.03 MB)

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