Dependence of the interfacial behavior of β-casein on phosphoserine residues

Journal of Dairy Science

Volumn 86, Issue 12, 2003, Pages 3876-3880

  Cassiano, M M ^a   Areas J A G ^a  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Dephosphorylated casein; Functional properties; Lipid protein interaction; Molecular dynamics

Indexed keywords

BOVINAE;

CASEIN; PHOSPHOSERINE;

ANIMAL; ARTICLE; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG STABILITY; EMULSION; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE;

ANIMALS; CASEINS; CATTLE; DRUG STABILITY; EMULSIONS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PHOSPHORYLATION; PHOSPHOSERINE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY;

EID: 4043068024     PISSN: 00220302     EISSN: None     Source Type: Journal    
DOI: 10.3168/jds.S0022-0302(03)73995-2     Document Type: Article

References (30)

1. 2H NMR and Molecular Modeling. Pages 193-201 in Magnetic Resonance in Food Science: A view to the Future. G. A. Webb, P. S. Belton, A. M. Gil, and I. Delgadillo, ed. The Royal Society of Chemistry, Cambridge, U.K.
2. Berendsen, H. J. C., J. P. M. Postma, W. F. van Gunsteren, A. DiNola, and J. R. Haak. 1984. Molecular dynamics with coupling to an external bath. J. Chem. Phys. 81:3684-3690.
3. Byler, D. M., H. M. Farrell, Jr., and H. Susi. 1988. Raman spectroscopic study of casein structure. J. Dairy Sci. 71:2622-2629.
4. Caessens, P. W. J. R., H. Gruppen, C. J. Slangen, S. Visser, and A. G. J. Vorangen. 1999. Functionality of β-casein peptides: importance of amphipathicity for emulsion-stabilizing properties. J. Agric. Food Chem. 47:1856-1862.
5. Cassiano, M. M., and J. A. G. Arêas. 2001. Study of bovine β-casein at water/lipid interface by molecular modeling. J. Mol. Struct. (Theochem) 539:279-288.
6. s1- and β- casein in solution. Arch. Biochem. Biophys. 211:689-696.
7. Eigel, W. N., J. E. Butler, C. A. Ernstrom, H. M. Farrell Jr., V. R. Harwalkar, R. Jenness, and R. McL. Whitney. 1984. Nomenclature of proteins of cow's milk: fifth revision. J. Dairy Sci. 67:1599-1631.
8. Farrell, H. M., Jr., P. X. Qi, E. M. Brown, P. H., Cooke, M. H. Tunick, E. D. Wickham, and J. J. Unruh. 2002. Molten globule structures in milk proteins: implications for potential new structure-function relationships. J. Dairy Sci. 85:459-471.
9. Graham, D. E., and M. C. Philips. 1979. Proteins at liquid interfaces. I. Kinetics of adsorption and surface denaturation. J. Colloid Interface Sci. 70:403-414.
10. Hill, S. E. 1996. Emulsions. Pages 153-185 in Methods of Testing Protein Functionality. G. M. Hall, ed. Blackie, London, U.K.
11. Husband, F. A., P. J. Wilde, A. R. Mackie, and M. J. Garrood. 1997. A comparison of the functional and interfacial properties of β-casein and dephosphorylated β-casein. J. Colloid Interface Sci. 195:77-85.
12. Jackson, J. D., 1975. Classical Electrodynamics. 2nd ed. Wiley, New York, NY.
13. de Jongh, H. H. J., and B. de Kruijff. 1990. The conformational changes of apocytochrome c upon binding to phospholipid vesicles and micelles of phospholipid based detergents: a circular dichroism study. Biochim. Biophys. Acta 1029:105-112.
14. Kabsch, W., and C. Sander. 1983. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
15. Kumosinski, T. F., E. M. Brown, and H. M. Farrell Jr. 1993. Three-dimensional molecular modeling of bovine caseins: an energy-minimized β-casein structure. J. Dairy Sci. 76:931-945.
16. Mundim, K. C., P. G. Pascutti, M. M. Cassiano, M. Loos, P. M. Bisch. 1998. THOR: a software package for molecular mechanics and dynamics simulations.
17. Pascutti, P. G., K. C. Mundim, A. S. Ito, and P. M. Bisch. 1999. Polarization effects of peptide conformations at water-membrane interface by molecular dynamics simulation. J. Comput. Chem. 20:971-982.
18. Press, W. H., S. A. Teukolsky, W. T. Vetterling, and B. P. Flannery. 1992. Numerical Receipes in Fortran. The Art of Scientific Computing. 2nd ed. Cambridge University Press, Cambridge, U.K.
19. Qi, P. X., E. M. Brown, and H. M. Farrell, Jr. 2001. 'New views' on structure-function relationships in milk proteins. Trends Food Sci. Technol. 12:339-346.
20. Rankin, S. E., A. Watts, and T. J. T. Pinheiro. 1998. Electrostatic and hydrophobic contributions to the folding mechanism of apocytochrome c driven by interaction with lipid. Biochemistry 37:12588-12595.
21. Reitz, J. R., F. J. Milford, and R. W. Christy. 1980. Foundations of Electromagnetism Theory. 3rd ed. Addison-Wesley, Reading, MA.
22. Ribadeau Dumas, B., G. Brignon, F. Grosclaude, and J.-C. Mercier. 1972. Structure primaire de la caséine β bovine. Séquence complète. Eur. J. Biochem. 25:505-514.
23. Sayle, R. A., and E. J. Milner-White. 1995. RASMOL: biomolecular graphics for all. Trends Biochem. Sci. 20:374-376.
24. Sood, S. M., and C. W. Slattery. 2000. Association of the quadruply phosphorylated β-casein from human milk with the nonphosphorylated form. J. Dairy Sci. 83:2766-2770.
25. Swaisgood, H. E. 1992. Chemistry of the Caseins. Pages 63-110 in Advanced Dairy Chemistry-1: Proteins. P. F. Fox, ed. Elsevier, London, U.K.
26. Swaisgood, H. E. 1993. Symposium: genetic perspectives on milk proteins: comparative studies and nomenclature. Review and update of casein chemistry. J. Dairy Sci. 76:3054-3061.
27. SYBYL: molecular modeling package. Tripos, Inc., St. Louis, MO.
28. van Gunsteren, W. F., and H. J. C. Berendsen. 1987. Groningen molecular simulation (GROMOS) library manual. Biomos, Groningen, The Netherlands.
29. van Gunsteren, W. F., and H. J. C. Berendsen. 1990. Computer simulation of molecular dynamics: methodology, applications, and perspectives in chemistry. Angew. Chem. Int. Ed. Engl. 29:992-1023.
30. van Hekken, D. L., and E. D. Strange. 1993. Functional properties of dephosphorylated bovine whole casein. J. Dairy Sci. 76:3384-3391.