Cultural advice

The Australian National University acknowledges, celebrates and pays our respects to the Ngunnawal and Ngambri people of the Canberra region and to all First Nations Australians on whose traditional lands we meet and work, and whose cultures are among the oldest continuing cultures in human history.

Aboriginal and Torres Strait Islander peoples are advised that ANU Library collections may include images, names, voices, and other representations of deceased persons.

Material in the collection may contain terms, language or views that reflect the period in which the item was created and may be considered inappropriate today.

Dephosphorylation of αs- and β -Caseins and Its Effect on Chaperone Activity: A Structural and Functional Investigation

Date

Authors

Koudelka, Tomas

Hoffmann, Peter

Carver, John

Publisher

American Chemical Society

Abstract

Milk casein proteins can act as molecular chaperones: under conditions of stress, such as elevated temperature, molecular chaperones stabilize proteins from unfolding, aggregating, and precipitating. In this study, αS- and β-caseins were dephosphorylate

Keywords

Keywords: alkaline phosphatase; casein; chaperone; article; chemistry; circular dichroism; metabolism; phosphorylation; physiology; protein folding; spectrofluorometry; static electricity; structure activity relation; Alkaline Phosphatase; Caseins; Circular Dichroi Amyloid fibril; Casein proteins; Molecular chaperone; Protein aggregation

URI

http://hdl.handle.net/1885/63193

Collections

ANU Research Publications

Source

Journal of Agricultural and Food Chemistry

Type

Journal article

DOI

10.1021/jf9008372

Restricted until

2037-12-31

Downloads

File

Description

01_Koudelka_Dephosphorylation_of_αs-_and__2009.pdf (1004.43 KB)

abcd