Phosphorylation quiz #1 Flashcards
Phosphorylation quiz #1
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What is phosphorylation, and how does it regulate protein function?
Phosphorylation is a post-translational modification involving the covalent attachment of a phosphate group to a protein, often using ATP as the phosphate donor. This modification can activate or deactivate the protein by altering its conformation, charge interactions, and hydrogen bonding, thereby regulating its function. Which enzymes are responsible for adding and removing phosphate groups during phosphorylation, and what are their specific roles?
Kinases are enzymes that add phosphate groups to proteins (phosphorylation), while phosphatases remove phosphate groups (dephosphorylation). Which amino acids are most commonly phosphorylated in eukaryotic cells, and why?
Serine, threonine, and tyrosine are most commonly phosphorylated in eukaryotic cells because they contain hydroxyl groups in their side chains, which can be replaced by phosphate groups. How does phosphorylation affect the properties of amino acids and proteins?
Phosphorylation increases the polarity and negative charge of amino acids, which can change protein conformation and activity by affecting charge interactions and hydrogen bonding. What is the primary source of phosphate groups used in phosphorylation reactions?
ATP (adenosine triphosphate) is the primary source of phosphate groups for phosphorylation, donating a phosphate and becoming ADP (adenosine diphosphate) in the process. What is phosphorylation and how does it regulate protein function?
Phosphorylation is the covalent attachment of a phosphate group to a protein, which can activate or deactivate the protein by altering its conformation and interactions. Which enzymes are responsible for adding and removing phosphate groups during phosphorylation?
Kinases add phosphate groups to proteins (phosphorylation), while phosphatases remove them (dephosphorylation). Which amino acids are most commonly phosphorylated in eukaryotic cells and why?
Serine, threonine, and tyrosine are most commonly phosphorylated because their side chains contain hydroxyl groups that can be replaced by phosphate groups. How does phosphorylation affect the properties of amino acids and proteins?
Phosphorylation increases the polarity and negative charge of amino acids, which can change protein conformation and activity by affecting charge interactions and hydrogen bonding. What is the primary source of phosphate groups used in phosphorylation reactions?
ATP (adenosine triphosphate) is the primary source, donating a phosphate group and becoming ADP (adenosine diphosphate) in the process.
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