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Coaggregation of κ-casein and β-lactoglobulin produces morphologically distinct amyloid fibrils

Raynes, J. K.; Day, L.; Crepin, Pauline; Horrocks, Mathew H.; Carver, John

Description

The unfolding, misfolding, and aggregation of proteins lead to a variety of structural species. One form is the amyloid fibril, a highly aligned, stable, nanofibrillar structure composed of β-sheets running perpendicular to the fibril axis. β-Lactoglobulin (β-Lg) and κ-casein (κ-CN) are two milk proteins that not only individually form amyloid fibrillar aggregates, but can also coaggregate under environmental stress conditions such as elevated temperature. The aggregation between β-Lg and κ-CN...[Show more]

CollectionsANU Research Publications
Date published: 2017
Type: Journal article
URI: http://hdl.handle.net/1885/217912
Source: Small
DOI: 10.1002/smll.201603591

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