C785 Biochemistry Module 3 Myoglobin and Hemoglobin Quiz 2020 – Western Governors University
25. What level of protein structure does hemoglobin have that is not found in myoglobin? 1. primary 2. secondary 3. tertiary 4. quaternary 10. Even though the amino acid sequence between subunits of hemoglobin and myoglobin are not exactly the same, there are other similarities between the two proteins. Which level of protein structure differs when comparing myoglobin to hemoglobin? 1. Primary 2. Secondary 3. Tertiary 4. Quaternary 43. As carbon monoxide binds to hemoglobin, the protein subunits change conformation to allow carbon monoxide to bind faster. This process is called __________. 1. non-competitive inhibition 2. allosteric binding 3. positive cooperativity 4. competitive inhibition 1. Which of the following accurately describes the functions of hemoglobin and myoglobin? 1. Hemoglobin transports oxygen, Myoglobin stores oxygen. 2. Hemoglobin stores oxygen, Myoglobin transports oxygen. 3. Hemoglobin transports CO2 and Myoglobin stores CO2 4. Myoglobin transports CO2 and Hemoglobin stores CO2 7. Hemoglobin and myoglobin proteins bind molecular oxygen. The protein subunit of hemoglobin does not bind directly to the oxygen. Instead, a specific atom binds oxygen. In hemoglobin, which of the following will directly bind oxygen? 1. Histidine 2. Heme 3. Carbon Monoxide 4. Iron 54. Which of the following also describes an "basic" condition? (Choose all that apply.) 1. low pH 2. high pH 3. low H+ 4. high H+ 5. low protons 6. high protons 20. Which one of the following statements about the graph is accurate? 1. The T state of hemoglobin is favored by low pH and induces the release of oxygen 2. The R state is the prevalent form of hemoglobin at low pH 3. The R state is favored by the low pH and induces the binding of oxygen 4. The T state of hemoglobin is favored by high pH and induces the release of oxygen 32. Acidosis occurs as a result of cardiac arrest. Which of the following is the theoretical reason why sodium bicarbonate might be administered to your patient during a cardiac arrest? 1. The bicarbonate acts to decrease pH, which enables hemoglobin to enter the T state and more effectively deliver oxygen to the tissues. 2. The bicarbonate acts to decrease pH, which enables hemoglobin to enter the lung and resume binding to oxygen. 3. The bicarbonate acts to increase pH, which may allow hemoglobin to transport oxygen more efficiently. 4. The bicarbonate acts to increase pH, prompting hemoglobin to shift to the R state and pick up CO2 that has accumulated during the cardiac arrest. 17. Myoglobin stores oxygen, whereas hemoglobin transports oxygen. Which of the following statements accurately describes the affinity of myoglobin and hemoglobin for oxygen? 1. Hemoglobin and myoglobin both have the same affinity for oxygen. 2. Hemoglobin has a higher affinity for oxygen compared to myoglobin. 3. Myoglobin has exactly one-quarter of the affinity for oxygen because it has only one subunit. 4. Myoglobin has a higher affinity for oxygen compared to hemoglobin. 39. Carbonic anhydrase is an important __________ present in the red blood cells that aids in efficient transportation of carbon dioxide in the form of _________, from tissues to lungs. 1. enzyme, carbon dioxide 2. substrate, bicarbonate ions 3. enzyme, bicarbonate ions 4. chemical, carbon monoxide 35. Oxygen binding alters the structure of an entire hemoglobin tetramer, so the structures of oxyhemoglobin and deoxyhemoglobin are noticeably different. The oxyhemoglobin conformation is specifically referred to as the __________ state, whereas the deoxyhemoglobin conformation is referred to as the __________ state. 1. Oxygenated and Deoxygenated 2. O and D 3. Relaxed and Tense 4. There is no difference between the two states
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43 as carbon monoxide binds to hemoglobin
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the protein subunits change conformation to allow carbon monoxide to bind faster this process is called 1 non competitive inhibition 2 allost