Skip to main content

Casein structures in the context of unfolded proteins

Journal Article


Download full-text (Open Access)

Abstract


  • Caseins were among the first proteins to be recognised as functional but unfolded. Many others are now known, providing better models of casein behaviour than either detergents or folded proteins. Caseins are members of a paralogous group of unfolded phosphoproteins, some of which share the ability to sequester amorphous calcium phosphate through phosphate centres. Non-covalent interactions of caseins can be through Pro- and Gln-rich sequences. Similar sequences in other unfolded proteins can also form open and highly hydrated structures such as gels, mucus and slimes. Many unfolded proteins, including κ- and αS2-caseins, can form amyloid fibrils under physiological conditions. The sequence-specific interactions that lead to fibrils can be reduced or eliminated by low specificity interactions among a mixture of caseins to yield, instead, amorphous aggregates. The size of amorphous whole casein aggregates is limited by the C-terminal half of κ-casein whose sequence resembles that of a soluble mucin.

Authors


  •   Thorn, David C. (external author)
  •   Ecroyd, Heath
  •   Carver, John A. (external author)
  •   Holt, Carl (external author)

Publication Date


  • 2015

Citation


  • Thorn, D. C., Ecroyd, H., Carver, J. A. & Holt, C. (2015). Casein structures in the context of unfolded proteins. International Dairy Journal, 46 2-11.

Scopus Eid


  • 2-s2.0-84927804854

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=3663&context=smhpapers

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/2643

Has Global Citation Frequency


Number Of Pages


  • 9

Start Page


  • 2

End Page


  • 11

Volume


  • 46

Place Of Publication


  • Netherlands

Abstract


  • Caseins were among the first proteins to be recognised as functional but unfolded. Many others are now known, providing better models of casein behaviour than either detergents or folded proteins. Caseins are members of a paralogous group of unfolded phosphoproteins, some of which share the ability to sequester amorphous calcium phosphate through phosphate centres. Non-covalent interactions of caseins can be through Pro- and Gln-rich sequences. Similar sequences in other unfolded proteins can also form open and highly hydrated structures such as gels, mucus and slimes. Many unfolded proteins, including κ- and αS2-caseins, can form amyloid fibrils under physiological conditions. The sequence-specific interactions that lead to fibrils can be reduced or eliminated by low specificity interactions among a mixture of caseins to yield, instead, amorphous aggregates. The size of amorphous whole casein aggregates is limited by the C-terminal half of κ-casein whose sequence resembles that of a soluble mucin.

Authors


  •   Thorn, David C. (external author)
  •   Ecroyd, Heath
  •   Carver, John A. (external author)
  •   Holt, Carl (external author)

Publication Date


  • 2015

Citation


  • Thorn, D. C., Ecroyd, H., Carver, J. A. & Holt, C. (2015). Casein structures in the context of unfolded proteins. International Dairy Journal, 46 2-11.

Scopus Eid


  • 2-s2.0-84927804854

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=3663&context=smhpapers

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/2643

Has Global Citation Frequency


Number Of Pages


  • 9

Start Page


  • 2

End Page


  • 11

Volume


  • 46

Place Of Publication


  • Netherlands