Protein Section Lecture #2 Part 2 - MC Flashcards
What is transamination?
A) The process of removing an amino group from an amino acid to make other substances.
B) The process of transferring an amine group from one amino acid to an intermediate to form a non-essential amino acid.
C) The linkage of two amino acids via a peptide bond through a condensation reaction.
D) The breaking of a dipeptide bond through a hydrolysis reaction.
B
Where does deamination typically occur in the body?
A) Kidneys
B) Liver
C) Heart
D) Brain
B
What is the outcome of a condensation reaction between two amino acids?
A) Formation of a dipeptide bond and a molecule of water.
B) Breakdown of a dipeptide bond using a water molecule.
C) Removal of an amino group to form ammonia.
D) Transfer of an amine group to a carboxylic acid group.
A
Which term describes a chain of fewer than 10 amino acids?
A) Dipeptide
B) Oligopeptide
C) Polypeptide
D) Protein
B
What defines the quaternary structure of a protein?
A) The sequence of amino acids linked by peptide bonds.
B) The alpha-helix and beta-pleated sheet formations.
C) The three-dimensional structure of a single polypeptide chain.
D) The three-dimensional structure formed by the interaction of multiple polypeptide chains.
D
What happens during protein denaturation?
A) Peptide bonds between amino acids are broken.
B) The primary structure of the protein is changed.
C) The three-dimensional structure of the protein is altered, usually permanently.
D) A new peptide bond is formed between amino acids.
C
How does a mutation in the DNA affect protein structure?
A) It alters the primary structure of the polypeptide, which can then affect higher levels of structure.
B) It denatures the protein, affecting its three-dimensional structure.
C) It removes amino groups from polypeptides, forming ammonia.
D) It causes the hydrolysis of peptide bonds within the protein.
A
