Conformation of β-casein B
References (23)
- et al.
Arch. Biochem. Biophys
(1955) - et al.
Biochim. Biophys. Acta
(1963) - et al.
Biochem. Biophys. Res. Commun
(1966) J. Dairy Sci
(1966)- et al.
J. Dairy Sci
(1965) - et al.
J. Biol. Chem
(1967) Acta Chem. Scand
(1965)Biochemistry
(1966)J. Dairy Res
(1963)- et al.
Neth. Milk Dairy J
(1964)
J. Am. Chem. Soc
Cited by (61)
Quantitative multivalent binding model of the structure, size distribution and composition of the casein micelles of cow milk
2022, International Dairy JournalCitation Excerpt :Reviews of the composition and properties of the casein micelles in milk have traditionally treated them as hydrophobic colloids (Atamer et al., 2017; Dalgleish & Corredig, 2012; de Kruif & Holt, 2003; Fox & Brodkorb, 2008; Holt, 1992; Horne, 2020; Mezzenga & Fischer, 2013; Rollema, 1992; Schmidt, 1982; Walstra, 1999; Waugh, 1971). Caseins are, undeniably, intrinsically disordered proteins (IDPs), as was originally recognised more than 70 years ago (Halwer, 1954; Herskovits, 1966; Kresheck, 1965; McMeekin, 1952; Noelken & Reibstein, 1968). In general, IDPs have an open and solvent-exposed conformation due to a predominantly hydrophilic sequence (Bowman et al., 2020; Schneider, Jensen, & Blackledge, 2019; van der Lee et al., 2014).
Self-association of bovine β-casein as influenced by calcium chloride, buffer type and temperature
2019, Food HydrocolloidsCitation Excerpt :The secondary structure of β-CN has been studied, although the exact structure remains elusive. For decades, β-CN was assumed to have a random coil structure, with little or no ordered secondary structure under physiological conditions (Andrews et al., 1979; Noelken & Reibstein, 1968). Holt and Sawyer (1993) put forward the ‘rheomorphic’ hypothesis, which states that casein has no fixed structure until aggregates are formed in response to calcium-binding by serine phosphate groups.
The caseins: Structure, stability, and functionality
2018, Proteins in Food Processing: Second EditionThe caseins: Structure, stability, and functionality
2017, Proteins in Food Processing, Second EditionThree-Dimensional Molecular Modeling of Bovine Caseins: An Energy-Minimized β-Casein Structure
1993, Journal of Dairy Science
- 1
Eastern Utilization Research and Development Division, Agricultural Research Service, U.S. Department of Agriculture.