As the value of p50 myoglobin for oxygen rises, it falls, rises, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls None of the aforementioned have a K _—- value, resulting in a strong affinity.
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As the value of p50 myoglobin for oxygen rises, it falls, rises, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls None of the aforementioned have a K _—- value, resulting in a strong affinity.
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- The following graph shows partial saturation (Y) of myoglobin (Mb), adult hemoglobin (HbA) and fetal hemoglobin (HbF) as a function of partial oxygen pressure (in mmHg). Use it to answer the question: Fetal hemoglobin ( biological function: HbF) demonstrates lower p50 than adult hemoglobin (HbA). This adaptation has the following A. Allow fetal hemoglobin form pentamer subunits. B. HbF has lower affinity for for O2 compared to adult Hb C. Allow fetal hemoglobin to effectively intercept oxygen from mother's hemoglobin. D. Allow fetal hemoglobin to replace myoglobin in musclesAfter spending a day or more at high altitude (with an oxygen partial pressure of 75 torr), the concentration of 2,3- bisphosphoglycerate (2,3-BPG) in red blood cells increases. What effect would an increased concentration of 2,3-BPG have on the oxygen-binding curve for hemoglobin? Why would this adaptation be beneficial for functioning well at high altitude?Which of the following statements is correct of BOTH haemoglobin and myoglobin? Acidic conditions increase the affinity for oxygen. The iron atom of the heme prosthetic group is bound to nitrogen atoms at five of six coordination sites. Four oxygen molecules bind to each subunit. Quaternary structure is found in both haemoglobin and myoglobin. Both haemoglobin and myoglobin show the same oxygen binding affinity at different
- Compare and contrast the oxygen binding pockets of myoglobin and haemoglobin.During strenuous exercise, the oxygen-hemoglobin dissociation curve shifts to the right. This rightward shift reflects an increase in the affinity of hemoglobin for oxygen and favors loading of O2 onto hemoglobin in the lungsThe shape for curve of oxygen binding to Myoglobin is ___________ and the shape for curve of oxygen binding to Hemoglobin is _________________ Hyperbolic, Hyperbolic Sigmoidal, Sigmoidal Flat, Sigmoidal Hyperbolic, Sigmoidal
- In addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin structure and function. Increases in blood H+ result in oxygen binding curves for hemoglobin that are shifted to the right. The effect of H+ can be understood in terms of the equilibrium:H-Hb+ + O2 → Hb-O2 + H+How does the difference in pH in the lungs and tissues help hemoglobin do its job of delivering oxygen? Use the equilibrium equation in your argument.Referring to the loading and unloading of oxygen from hemoglobin (as illustrated in the figure), which of the following statements is correct? Oxygen Dissociation Curve.png Group of answer choices When a person in ventilating at rest, 75% of hemoglobin is still oxyhemoglobin The percent saturation of hemoglobin is higher at higher partial pressures of oxygen A decrease in the pH of the blood would promote unloading oxygen from the hemoglobin All of these are correctDescribe the differences in the oxygen-binding properties of hemoglobin and myoglobin.
- Oxygen-binding proteins myoglobin and hemoglobin require the prosthetic group ______.Which of the following is not true with regards to the oxygen-hemoglobin curve?Which of the following combinations would all result in an increase in stimulation to breathe? Group of answer choices decrease in PCO2 : increase in H+ : decrease in PO2 increase in PCO2 : increase in H+ : decrease in PO2 decrease in PCO2 : decrease in H+ : decrease in PO2 increase in PCO2 : decrease in H+ : increase in PO2 decrease in PCO2 : decrease in H+ : increase in PO2