BioChem C785 - WGU - Module 3 – with all Questions and Answers 100% Correct

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BioChem C785 - WGU - Module 3 – with all Questions and Answers 100% Correct Addition of oxygen alters the shape of the iron-heme complex, and therefore its absorption of light as indicated by its... color change from dark purple (the color of hemoglobin in venous blood) to brilliant scarlet (the color of hemoglobin in arterial blood). Correct Answer- True As carbon monoxide binds to hemoglobin, the protein subunits change conformation to allow carbon monoxide to bind faster, This process is called Correct Answer- positive cooperatively Bohr effect is a relationship between hemoglobin's oxygen binding behavior in conjunction with the pH of the surroundings. When the pH is high, hemoglobin has high affinity for oxygen and binds oxygen. Correct Answer- True BPG stabilizes the T (tense) states of hemoglobin Correct Answer- True Carbon monoxide outcompetes oxygen for attachment to the heme group of hemoglobin where it is permanently, covalently attached. Correct Answer- True Carbon monoxide shifts the oxygen-hemoglobin dissociation curve to the left, while carbon dioxide shifts this curve to the right. Based on your knowledge of the Bohr Effect, what is true? Correct Answer- Carbon dioxide decreases the hemoglobin's affinity for oxygen, while carbon monoxide increases it. Carbonic anhydrase is an important enzyme present in the red blood cells that aids in efficient transportation of carbon dioxide in the form of bicarbonate ions, from tissues to lungs. Correct Answer- True Cooperatively refers to Correct Answer- structural changes that increases the affinity for oxygen in hemoglobin Even though the amino acids 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 is not found in both molecules? Correct Answer- Quarternary Fetal hemoglobin binds to oxygen tightly at lower oxygen concentrations since its R state is the preferred structure. Correct Answer- True Hb (hemoglobin) binds to CO (carbon monoxide) with a higher affinity than oxygen and stabilizes the R (relaxed) state Correct Answer- True Hemoglobin acts as a buffer and controls the pH of the blood by binding to h+ ions. Correct Answer- True Hemoglobin and myoglobin proteins bind to molecular oxygen. However, the protein part of the hemoglobin does not bind directly to the oxygen. Instead a specific atom helps bind the oxygen - Correct Answer- Iron Hemoglobin consists of 4 protein subunits. Each subunit contains a heme group that holds an iron atom, which can bind to: Correct Answer- an oxygen molecule Hemoglobin is an oxygen transport protein, whereas myoglobin is an oxygen storage protein. They exhibit different binding curves when plotted on a graph with total partial pressure of the oxygen (x-axis) plotted against the percentage saturation of hemoglobin (y-axis). What pattern of binding curves do these proteins exhibit? Correct Answer- Hemoglobin has a sigmoidal curve whereas the myoglobin has a hyperbolic curve. Hemoglobin's cooperative binding behavior is key to its physiological function, the binding of which molecules influences this behavior? Correct Answer- Oxygen Hemoglobins ability to bind or release oxygen depends on the pH of the environment. This behavior is known as the Bohr Effect, thus Hemoglobin binds to the oxygen at high pH and releases oxygen at a low pH. Correct Answer- True In a firefighter who is brought to the emergency room after entering a burning building, the planar confirmation of the heme group in hemoglobin is preferred Correct Answer- True In comparison to adult hemoglobin, fetal hemoglobin has a higher affinity for oxygen because it doesn't bind 2,3-BPG. Correct Answer- True In the deoxygenated state the heme is bent, where as in the oxygenated state, the heme is planar. Correct Answer- True In the locations where the pH is low, hemoglobin will be in the T state, allowing it to release oxygen more effectively Correct Answer- Tr [Show More]

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