Dephosphorylation of αs- and β-Caseins and Its Effect on Chaperone Activity: A Structural and Functional Investigation
Author:
Affiliation:
1. School of Chemistry and Physics
2. Adelaide Proteomics Centre, School of Molecular and Biomedical Science
3. The University of Adelaide, Adelaide, South Australia 5005, Australia
Publisher
American Chemical Society (ACS)
Subject
General Agricultural and Biological Sciences,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jf9008372
Reference43 articles.
1. Why are ?natively unfolded? proteins unstructured under physiologic conditions?
2. Alpha(S1)-casein is required for the efficient transport of beta- and kappa-casein from the endoplasmic reticulum to the Golgi apparatus of mammary epithelial cells
3. Molecular Chaperone-like Properties of an Unfolded Protein, αs-Casein
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