Koudelka, TomasHoffmann, PeterCarver, John2015-12-100021-8561http://hdl.handle.net/1885/63193Milk 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 dephosphorylateKeywords: 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 aggregation200910.1021/jf90083722016-02-24