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Related Concept Videos

Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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Related Experiment Video

Updated: Jul 1, 2026

Sigma's Non-specific Protease Activity Assay - Casein as a Substrate
11:37

Sigma's Non-specific Protease Activity Assay - Casein as a Substrate

Published on: September 17, 2008

Heat-induced changes in casein-derived phosphopeptides.

H Meisel1, H B Andersson, K Buhl

  • 1Institute for Chemistry and Physics, Federal Dairy Research Centre, Kiel, FRG.

Zeitschrift Fur Ernahrungswissenschaft
|September 1, 1991
PubMed
Summary
This summary is machine-generated.

Heating bovine sodium caseinate causes dephosphorylation of casein phosphopeptides, reducing their solubility. This heat-induced degradation impacts their potential as nutrient carriers.

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Area of Science:

  • Food Chemistry
  • Protein Chemistry
  • Nutritional Science

Background:

  • Casein phosphopeptides are known to bind calcium and trace elements.
  • Understanding heat-induced changes is crucial for food processing and nutritional value.

Purpose of the Study:

  • To investigate heat-induced changes in tryptic phosphopeptides from bovine sodium caseinate.
  • To assess the impact of heating on the solubility and integrity of these phosphopeptides.

Main Methods:

  • Bovine sodium caseinate was used as a model system.
  • Samples were subjected to microwave and oven heating.
  • Tryptic hydrolysis and analysis of soluble and insoluble fractions were performed.

Main Results:

  • Both heating methods caused significant dephosphorylation (loss of peptide-bound phosphorus).
  • Heating decreased the concentration of casein-phosphopeptides in the soluble tryptic hydrolysate.
  • Lysinoalanyl-casein was predominantly found in the pH 4.6-insoluble fraction.

Conclusions:

  • Hydrolysis of phosphoseryl to seryl residues is the primary degradation pathway for soluble products.
  • Heat treatment alters the functional properties of casein phosphopeptides, affecting their nutrient carrier potential.