5 Questions
Which protein has a very long lifespan?
Hemoglobin
What determines protein stability according to the text?
N-terminal amino acid residues
Which enzyme cleaves the internal peptide bonds in which the carboxylic group is of aromatic amino acids or leucine?
Pepsin
Which cells produce pepsinogen?
Chief cells
What activates trypsinogen to form trypsin?
Enteropeptidase
Study Notes
Protein Longevity and Stability
- Ubiquitin has a very long lifespan due to its highly conserved sequence and lack of lysine residues, making it resistant to proteolytic degradation.
Protein Stability Determinants
- The stability of a protein is determined by its amino acid sequence, with certain sequences being more prone to degradation than others.
Peptide Bond Cleavage
- Cathepsin D is the enzyme responsible for cleaving internal peptide bonds in which the carboxylic group is of aromatic amino acids or leucine.
Pepsinogen Production
- Pepsinogen is produced by chief cells in the stomach.
Trypsin Activation
- Enterokinase activates trypsinogen to form trypsin.
Test your knowledge of protein turnover, catabolism of amino acids, and protein digestion with this biochemistry quiz. Learn about the synthesis and degradation of proteins, as well as the factors that determine protein stability.
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