lOMoARcPSD|336 891 29 UNE BIOCHEMISTRY MIDTERM EXAM 2024 -
2025/LATEST UPDATE ACTUAL EXAM WITH CORRECT DETAILED AND VERIFIED ANSWERS/A+ GRADE How do most enzymes reduce the activation energy needed to move a reaction forward? Providing an active site most complementary the transition state An enzyme has a mutation within the substrate binding of the coenzyme needed for covalent catalysis. Which of the following is likely to result as a consequence of this mutation? The enzyme will not be able to form the transition state complex Hemoglobin has the ability to display cooperative binding while myoglobin does not display this binding kinetic pattern. Which of the following di昀昀erences between the two proteins accounts for this di昀昀erence in binding kinetics? The presence of quaternary structure in hemoglobin Cleavage of fructose 1,6-bisphosphate to dihydroxy and glyceraldehyde 3-phosphate is achieved by what class of enzymes? Lyase Domains are common structural elements that retain a particular function within the protein. Which of the following is an example of a protein domain? An arrangement of beta strands connected to alpha helices (BaBaB) Covalent catalysis is used by many enzymes to cleave peptide bonds. Which of the lOMoARcPSD|336 891 29 following amino acids would not facilitate this type of catalysis? Valine Which of the following proteins is likely to have quaternary structure? A multimeric protein that contains multiple peptide chains What of the following best describes a protein domain? A relatively large pattern a three -dimensional structure that is recognized across many proteins Movement of ammonia from an amino acid to an a-keto acid involved a family of enzymes best categorized as which of the following? Tranferases A 19 -year-old boy is diagnosed with Creutzfeldt -Jakob Disease which is caused by the introduction of an amyloid fold in the disease -causing protein. The introduction of this fold causes the protein to transition from a primarily a-helix structure to an aggregate of mostly B- sheets. This change in protein structure (leading to disease) is best attributed to changes in which of the following? Folding of the secondary structures Chymotropsin is a protease that cleaves peptide bonds. It is characterized as which lOMoARcPSD|336 891 29 of the following classes of enzymes? Hydrolases Which of the following best describes tertiary structure? Interactions between single amino acids adjacent to one another Hemoglobin has the ability to display cooperative binding while myoglobin does not display this binding pattern. Which of the following di昀昀erences between the two proteins accounts for the di昀昀erence in binding kinetics? The presence of quaternary structure in hemoglobin Chan ges in the physiological variables listed below can alter the a昀케nity of hemoglobin for oxygen. Which of the following will lower the a昀케nity of hemoglobin for oxygen? Increase in 2,3 bisphosphoglycerate (BPG) An enzyme has a mutation within the substrate binding site that reduces the binding of the coenzyme needed for covalent catalysis. Which of the following is likely to result as a consequence of this mutation? The enzyme will not be able to form the transition state complex An enzyme is participating in a general acid-base catalysis reaction with an optimal reaction pH of 6.0. If acid is added to the environment reducing the pH to
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