Detail the similarities and differences between myoglobin and hemoglobin structure.
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Q: How does the fetal hemoglobin differ from the maternal hemoglobin in regards to structure and…
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Q: How many atoms of oxygen can be bound to a singlemolecule of hemoglobin?
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Q: Graph the relationship between hemoglobin–O2 saturation and the partial pressure of O2 in the blood.…
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Q: a.What is the difference between the 5th and 6 coordination sites in the heme group?
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Q: Identify the factors that shift the oxyhemoglobin dissociation curve to the left?
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Q: 30. assicuatuib if 2alpha and 2 beta chains to form adult hemoglobin
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Q: Why is oxygen efficiently transferred from hemoglobin in theblood to myoglobin in the muscles?
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Q: Define how carbaminohemoglobin (HbCO2) is formed ?
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Q: L List two similarities and two differences between hemoglobin and myoglobin.
A: The sequence of amino acids in a polypeptide refers to the primary structure of protein. The…
Q: Contrast the structures of the proteins myoglobin and hemoglobin.
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Q: Calculate the fractional saturation for hemoglobin when the partial pressure of oxygen is 80 mm Hg.…
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Q: . With regard to how mountain climbers adapt to the low oxygen pressure of higher altitudes, explain…
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Q: Why is it advantageous for the oxygen-hemoglobindissociation curve to shift to the left in the lungs…
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Q: What other diseases are associated with estraneous forms of hemoglobin subunits in the human adult?
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Q: 22. Please provide a biological explanation for why fetal hemoglobin has evolved to have lower…
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Q: Identify the factors that shift the oxyhemoglobin dissociation curve to the right?
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Q: What is the physiological significance of the cooperative binding of oxygen by hemoglobin?
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Q: the structure and functions of hemoglobin and the three determinants for how much oxygen is bound
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Q: Why does hemoglobin have high affinity for oxygen in arterial blood and lower affinity in…
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A:
Q: Compare and contrast the oxygen binding pockets of myoglobin and haemoglobin.
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Q: Discuss the factors that affect oxygen binding in hemoglobin.
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Q: What are the geometrical and conformational changes the hemoglobin undergoes on binding of 1st…
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Q: What color is deoxyhemoglobin? Why?
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Q: The following statement describes which level of structure of the hemoglobin molecule? "Each chain…
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Q: How much iron is there in the hemoglobin of a 70-kg adult? Assume that the blood volume is 70 ml…
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Q: How does the oxygen-binding curve of fetal hemoglobin differ from that of adult hemoglobin?
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4.2 Detail the similarities and differences between myoglobin and hemoglobin structure.
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- The primary and tertiary structures of hemoglobin and myoglobin are very similar and both contain the 'heme' group as an oxygen-binding prosthetic group. However this There are important functional differences between the two proteins. Hemoglobin oxygen transport protein, myoglobin functions as oxygen storage protein. Hemoglobin and consider the structural differences and oxygen binding curves between myoglobin why myoglobin is a good oxygen transport protein, while hemoglobin Explain why it cannot be a good oxygen storage protein.Why chemical change occurs in the primary structure of the globin portionof the hemoglobin molecule ?What is the difference between oxyhemoglobin and reduced hemoglobin in terms of structure?
- Contrast the structures of the proteins myoglobin and hemoglobin.What is the difference between the T form and R form of the hemoglobin molecule?Compare the structure and function of hemoglobin and myoglobin. Which oxygen binding curve in the graph below belongs to myoglobin and which to hemoglobin? Please specify. Explain the effect of pH on oxygen binding to hemoglobin, and show on the graph in which direction the pH will shift if it falls below the physiological pH value (7.4).
- Explain how the binding of molecular oxygen (O2) to haemoglobin affects the tertiary structures of each monomer. Hence, explain how this influences the quaternary structure of the haemoglobin molecule, and how this helps haemoglobin to transport O2 from the lungs to the muscles.Describe the structure of hemoglobin and How does the structure of hemoglobin allow it to combine with oxygen?Which of the followingstatement is FALSE about myoglobin? Select one: a) Oxygen dissociation curve for myoglobin is non-sigmoidal b)It has only one hemocyanin for anaerobic respiration c) It has higher affinity for oxygen even at high partial pressure of carbon dioxide d)It can be found in the skeletal muscle tissue
- what is main difference between myoglobin and hemogloin and in what situations/circumstancees are each used and why?Describe the structural basis for the cooperative (allosteric) binding of O2 by hemoglobin but not by myoglobinThe differences between hemoglobin and myoglobin include a) hemoglobin exhibits a lower degree of O2 saturation at all physiologically relevant partial pressures of O2 than does myoglobin. b) all of the answers arecorrect. c) hemoglobin is a tetramer whereas myoglobin is a monomer. O d) hemoglobin exhibits O2 binding cooperativity while myoglobin does not.