Coaggregation of κ-casein and β-lactoglobulin produces morphologically distinct amyloid fibrils
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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]
Collections | ANU Research Publications |
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Date published: | 2017 |
Type: | Journal article |
URI: | http://hdl.handle.net/1885/217912 |
Source: | Small |
DOI: | 10.1002/smll.201603591 |
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