CHEM 1005 Midterm Exam 2024 Questions & Answers 100% (RATED A+)

Changes in the physiological variables listed below can alter the affinity of hemoglobin for oxygen. Which of the following will lower the affinity of hemoglobin for oxygen? - ANSWERSIncrease in 2,3 bisphosphoglycerate (BPG) A decreased affinity will increase the rate of oxygen delivery to the tissues. This will occur when pH is low, there is an increase in CO2, protons or 2,3 BPG. The other scenarios (a, c, d) will all increase the affinity for O2. Which of the following proteins is likely to have quaternary structure? - ANSWERSA multimeric protein that contains multiple peptide chains Primary structure is the largely unfolded strand of amino acids, while β- sheets and α-helices are examples of secondary structures. How these structures interact would be an example of tertiary structure. Quaternary structure is a characteristic of interactions between several individual polypeptide chains. Chymotrypsin is a protease that cleaves peptide bonds. It is characterized as which of the following classes of enzymes? - ANSWERSHydrolases Review the 6 classes of enzymes. Peptide bonds are cleaved and water is released in the reaction. How do most enzymes reduce the activation energy needed to move a reaction forward? - ANSWERSProviding an active site most complementary the transition state In the induced fit model, the active site is more homologous to the transition state of the reaction and this reduces the activation energy of the transition. 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? - ANSWERSThe enzyme will not be able to form the transition state complex Loss of coenzyme binding will result in inability to form the transition substrate enzyme complex. α-helices and β-sheets are primarily stabilized by which of the following interactions? - ANSWERSHydrogen bonding A