Match the colour of myoglobin to the ligand bound. brown red pink 1. carbon monoxide 2. nitric oxide 3. water
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- The iron-carrying protein that assists in the transport of oxygen into muscle cells is? A. Myoglobin B. Hematocrit C. Hemoglobin D. Heme groupExplain how the structure of myoglobin changes upon oxygen binding.At low pO2, Myoglobin’s O2 binding affinity is ______ that of Hb. a essentially the same as b higher than c lower than
- Which statement is true for the heme group present myoglobin: a. Oxygen binding to heme group is influenced by serine residues within proteins’ sequences. b. Oxygen binding to heme can become irreversible as a result of interaction with certain protein residues. c. Oxygen reversibly binds to the heme prostetic group and this binding is influenced by histidine residues within the myoglobin sequence. d. The heme group dissociates from Mb after oxygen is released.Does myoglobin have the same high affinity for CO as hemoglobin?Compare and contrast the oxygen binding pockets of myoglobin and haemoglobin.
- Which of the following is true about the proximal histidine of hemoglobin? A. It forms a hydrogen bond with bound oxygen. B. It is bonded to the Fe2+ atom coordinated by heme C. It binds oxygen D. It is not consumed in myoglobinAs 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.One of your friends has anemia. They consistently complain of higher levels of fatigue when you go for runs or exercise. What is the cause of this? Decreased oxygen carrying capacity of myoglobin Decreased muscle spindle activation of the gastroc Increased use of fast twitch muscle fibers Decreased oxygen carrying capacity of hemoglobin
- 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 differentExplain how the change of a single amino acid in hemoglobin leads to the aggregation of hemoglobin into long fibers.increase the affinity”, “decrease the affinity” or “no change in affinity i) Myoglobin ii) Haemoglobin when A decrease in the partial pressure of CO2 in the lungs An increase in the BPG level
