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What is the main function of hemoglobin?
What is the essential prosthetic group found in hemoglobin and myoglobin?
How many polypeptide chains make up hemoglobin A?
What is the difference between hemoglobin and myoglobin in terms of oxygen binding?
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What is the oxygen dissociation curve?
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What is P50 in the oxygen dissociation curve?
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What is the T form of hemoglobin?
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What is the physiological adaptation to high altitude?
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What is the variant of the β chain found in fetal hemoglobin?
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What is the Bohr effect?
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What happens when carbon monoxide (CO) binds to the hemoglobin iron?
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How many iron atoms are present in heme?
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What is the main function of hemoglobin?
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What is the essential prosthetic group found in hemoglobin and myoglobin?
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How many polypeptide chains make up hemoglobin A?
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What is the difference between hemoglobin and myoglobin in terms of oxygen binding?
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What is the oxygen dissociation curve?
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What is P50 in the oxygen dissociation curve?
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What is the T form of hemoglobin?
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What is the physiological adaptation to high altitude?
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What is the variant of the β chain found in fetal hemoglobin?
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What is the Bohr effect?
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What happens when carbon monoxide (CO) binds to the hemoglobin iron?
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How many iron atoms are present in heme?
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What is the main function of hemoglobin?
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What is the prosthetic group contained in both hemoglobin and myoglobin?
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What is the difference between hemoglobin and myoglobin in terms of oxygen binding?
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What is P50?
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What is the difference between the T and R forms of hemoglobin?
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What is the physiological adaptation to high altitude?
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What is the variant of the β chain in fetal hemoglobin?
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What is the Bohr effect?
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What is the effect of carbon monoxide (CO) on hemoglobin?
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What is the difference in structure between hemoglobin A and myoglobin?
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What is the state of the iron atom in heme that binds oxygen?
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What is the main function of hemoglobin?
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What is the essential prosthetic group found in hemoglobin and myoglobin?
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How many oxygen molecules can hemoglobin bind?
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What is P50 in the oxygen dissociation curve?
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What is the deoxy form of hemoglobin called?
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What is the physiological adaptation to high altitude?
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What is the variant of the β chain found in fetal hemoglobin?
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What is the effect of low pH on the release of oxygen from hemoglobin?
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What is the effect of increased pCO2 on the release of oxygen from hemoglobin?
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What is the name of the compound formed when CO binds to the hemoglobin iron?
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What is the oxygen-binding capacity of myoglobin compared to hemoglobin?
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What is the structural difference between hemoglobin and myoglobin?
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What is the main function of hemoglobin?
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What is the essential prosthetic group found in both hemoglobin and myoglobin?
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How many polypeptide chains make up hemoglobin A?
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Which state of the iron atom in heme can bind oxygen?
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How many oxygen molecules can hemoglobin bind?
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What is P50 in the oxygen dissociation curve?
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What is the deoxy form of hemoglobin called?
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What is the physiological adaptation to high altitude?
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What is the variant of the β chain found in fetal hemoglobin?
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What is the Bohr effect?
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What happens when carbon monoxide (CO) binds to the hemoglobin iron?
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What is the main function of hemoglobin?
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What is the essential prosthetic group contained in hemoglobin and myoglobin?
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What is the difference between the structure of hemoglobin and myoglobin?
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What is the role of heme in oxygen binding?
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How many oxygen molecules can hemoglobin bind?
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What is the P50 value in the oxygen dissociation curve?
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What is the physiological adaptation to high altitude?
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What is the difference between fetal and adult hemoglobin?
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What is the Bohr effect?
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What is the effect of carbon monoxide on hemoglobin?
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What is the difference between the deoxy and oxygenated forms of hemoglobin?
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Study Notes
Structure and Function of Oxygen Transport Proteins
- Oxygen is essential for cellular respiration and is poorly soluble in plasma, making it impossible to transport by simple diffusion.
- Hemoglobin is found exclusively in red blood cells and its main function is to transport oxygen from the lungs to the capillaries of the tissues.
- Hemoglobin and myoglobin are two proteins that contain the essential prosthetic group heme, which contains an iron atom.
- Hemoglobin A is composed of four polypeptide chains held together by noncovalent interactions, while myoglobin consists of a single polypeptide chain structurally similar to the individual subunit polypeptide chains of hemoglobin.
- Heme is composed of a ringlike organic compound known as a porphyrin, to which an iron atom is attached, and the ferrous(+2) state binds oxygen while the ferric state (3+) cannot bind oxygen.
- Myoglobin can bind only one molecule of oxygen, while hemoglobin can bind four oxygen molecules, one at each of its four heme groups.
- The oxygen dissociation curve is a plot of saturation measured at different partial pressures of oxygen (pO2), and P50 is the partial pressure of O2 (PO2) at which the protein is half-saturated with O2.
- The deoxy form of hemoglobin is called the "T" or taut form, while the oxygenated form is called the "R" or relaxed form, and cooperative binding of oxygen by the four subunits of hemoglobin means that the binding of an oxygen molecule at one heme group increases the oxygen affinity of the remaining heme groups in the same hemoglobin molecule.
- The physiological adaptation to high altitude involves increased tissue concentrations of 2,3-BPG, which lowers the oxygen affinity of hemoglobin, permitting greater unloading of oxygen in the capillaries of the tissues.
- Fetal hemoglobin contains a variant of the β chain, called ɤ (gamma), which has a His→Ser substitution in the 2,3-BPG-binding site, resulting in an enhanced O2-binding affinity that allows transfer of O2 from the maternal to the fetal red blood cells.
- The release of oxygen from hemoglobin is enhanced when the pH is lowered or when the hemoglobin is in the presence of an increased pCO2, a phenomenon known as the Bohr effect.
- Carbon monoxide (CO) binds tightly (but reversibly) to the hemoglobin iron, forming carboxyhemoglobin, which shifts the oxygen dissociation curve to the left and changes the normal sigmoidal shape toward a hyperbola, resulting in the affected hemoglobin being unable to release oxygen to the tissues.
Structure and Function of Oxygen Transport Proteins
- Oxygen is essential for cellular respiration and is poorly soluble in plasma, making it impossible to transport by simple diffusion.
- Hemoglobin is found exclusively in red blood cells and its main function is to transport oxygen from the lungs to the capillaries of the tissues.
- Hemoglobin and myoglobin are two proteins that contain the essential prosthetic group heme, which contains an iron atom.
- Hemoglobin A is composed of four polypeptide chains held together by noncovalent interactions, while myoglobin consists of a single polypeptide chain structurally similar to the individual subunit polypeptide chains of hemoglobin.
- Heme is composed of a ringlike organic compound known as a porphyrin, to which an iron atom is attached, and the ferrous(+2) state binds oxygen while the ferric state (3+) cannot bind oxygen.
- Myoglobin can bind only one molecule of oxygen, while hemoglobin can bind four oxygen molecules, one at each of its four heme groups.
- The oxygen dissociation curve is a plot of saturation measured at different partial pressures of oxygen (pO2), and P50 is the partial pressure of O2 (PO2) at which the protein is half-saturated with O2.
- The deoxy form of hemoglobin is called the "T" or taut form, while the oxygenated form is called the "R" or relaxed form, and cooperative binding of oxygen by the four subunits of hemoglobin means that the binding of an oxygen molecule at one heme group increases the oxygen affinity of the remaining heme groups in the same hemoglobin molecule.
- The physiological adaptation to high altitude involves increased tissue concentrations of 2,3-BPG, which lowers the oxygen affinity of hemoglobin, permitting greater unloading of oxygen in the capillaries of the tissues.
- Fetal hemoglobin contains a variant of the β chain, called ɤ (gamma), which has a His→Ser substitution in the 2,3-BPG-binding site, resulting in an enhanced O2-binding affinity that allows transfer of O2 from the maternal to the fetal red blood cells.
- The release of oxygen from hemoglobin is enhanced when the pH is lowered or when the hemoglobin is in the presence of an increased pCO2, a phenomenon known as the Bohr effect.
- Carbon monoxide (CO) binds tightly (but reversibly) to the hemoglobin iron, forming carboxyhemoglobin, which shifts the oxygen dissociation curve to the left and changes the normal sigmoidal shape toward a hyperbola, resulting in the affected hemoglobin being unable to release oxygen to the tissues.
Structure and Function of Oxygen Transport Proteins
- Oxygen is essential for cellular respiration and is poorly soluble in plasma, making it impossible to transport by simple diffusion.
- Hemoglobin is found exclusively in red blood cells and its main function is to transport oxygen from the lungs to the capillaries of the tissues.
- Hemoglobin and myoglobin are two proteins that contain the essential prosthetic group heme, which contains an iron atom.
- Hemoglobin A is composed of four polypeptide chains held together by noncovalent interactions, while myoglobin consists of a single polypeptide chain structurally similar to the individual subunit polypeptide chains of hemoglobin.
- Heme is composed of a ringlike organic compound known as a porphyrin, to which an iron atom is attached, and the ferrous(+2) state binds oxygen while the ferric state (3+) cannot bind oxygen.
- Myoglobin can bind only one molecule of oxygen, while hemoglobin can bind four oxygen molecules, one at each of its four heme groups.
- The oxygen dissociation curve is a plot of saturation measured at different partial pressures of oxygen (pO2), and P50 is the partial pressure of O2 (PO2) at which the protein is half-saturated with O2.
- The deoxy form of hemoglobin is called the "T" or taut form, while the oxygenated form is called the "R" or relaxed form, and cooperative binding of oxygen by the four subunits of hemoglobin means that the binding of an oxygen molecule at one heme group increases the oxygen affinity of the remaining heme groups in the same hemoglobin molecule.
- The physiological adaptation to high altitude involves increased tissue concentrations of 2,3-BPG, which lowers the oxygen affinity of hemoglobin, permitting greater unloading of oxygen in the capillaries of the tissues.
- Fetal hemoglobin contains a variant of the β chain, called ɤ (gamma), which has a His→Ser substitution in the 2,3-BPG-binding site, resulting in an enhanced O2-binding affinity that allows transfer of O2 from the maternal to the fetal red blood cells.
- The release of oxygen from hemoglobin is enhanced when the pH is lowered or when the hemoglobin is in the presence of an increased pCO2, a phenomenon known as the Bohr effect.
- Carbon monoxide (CO) binds tightly (but reversibly) to the hemoglobin iron, forming carboxyhemoglobin, which shifts the oxygen dissociation curve to the left and changes the normal sigmoidal shape toward a hyperbola, resulting in the affected hemoglobin being unable to release oxygen to the tissues.
Structure and Function of Oxygen Transport Proteins
- Oxygen is essential for cellular respiration and is poorly soluble in plasma, making it impossible to transport by simple diffusion.
- Hemoglobin is found exclusively in red blood cells and its main function is to transport oxygen from the lungs to the capillaries of the tissues.
- Hemoglobin and myoglobin are two proteins that contain the essential prosthetic group heme, which contains an iron atom.
- Hemoglobin A is composed of four polypeptide chains held together by noncovalent interactions, while myoglobin consists of a single polypeptide chain structurally similar to the individual subunit polypeptide chains of hemoglobin.
- Heme is composed of a ringlike organic compound known as a porphyrin, to which an iron atom is attached, and the ferrous(+2) state binds oxygen while the ferric state (3+) cannot bind oxygen.
- Myoglobin can bind only one molecule of oxygen, while hemoglobin can bind four oxygen molecules, one at each of its four heme groups.
- The oxygen dissociation curve is a plot of saturation measured at different partial pressures of oxygen (pO2), and P50 is the partial pressure of O2 (PO2) at which the protein is half-saturated with O2.
- The deoxy form of hemoglobin is called the "T" or taut form, while the oxygenated form is called the "R" or relaxed form, and cooperative binding of oxygen by the four subunits of hemoglobin means that the binding of an oxygen molecule at one heme group increases the oxygen affinity of the remaining heme groups in the same hemoglobin molecule.
- The physiological adaptation to high altitude involves increased tissue concentrations of 2,3-BPG, which lowers the oxygen affinity of hemoglobin, permitting greater unloading of oxygen in the capillaries of the tissues.
- Fetal hemoglobin contains a variant of the β chain, called ɤ (gamma), which has a His→Ser substitution in the 2,3-BPG-binding site, resulting in an enhanced O2-binding affinity that allows transfer of O2 from the maternal to the fetal red blood cells.
- The release of oxygen from hemoglobin is enhanced when the pH is lowered or when the hemoglobin is in the presence of an increased pCO2, a phenomenon known as the Bohr effect.
- Carbon monoxide (CO) binds tightly (but reversibly) to the hemoglobin iron, forming carboxyhemoglobin, which shifts the oxygen dissociation curve to the left and changes the normal sigmoidal shape toward a hyperbola, resulting in the affected hemoglobin being unable to release oxygen to the tissues.
Structure and Function of Oxygen Transport Proteins
- Oxygen is essential for cellular respiration and is poorly soluble in plasma, making it impossible to transport by simple diffusion.
- Hemoglobin is found exclusively in red blood cells and its main function is to transport oxygen from the lungs to the capillaries of the tissues.
- Hemoglobin and myoglobin are two proteins that contain the essential prosthetic group heme, which contains an iron atom.
- Hemoglobin A is composed of four polypeptide chains held together by noncovalent interactions, while myoglobin consists of a single polypeptide chain structurally similar to the individual subunit polypeptide chains of hemoglobin.
- Heme is composed of a ringlike organic compound known as a porphyrin, to which an iron atom is attached, and the ferrous(+2) state binds oxygen while the ferric state (3+) cannot bind oxygen.
- Myoglobin can bind only one molecule of oxygen, while hemoglobin can bind four oxygen molecules, one at each of its four heme groups.
- The oxygen dissociation curve is a plot of saturation measured at different partial pressures of oxygen (pO2), and P50 is the partial pressure of O2 (PO2) at which the protein is half-saturated with O2.
- The deoxy form of hemoglobin is called the "T" or taut form, while the oxygenated form is called the "R" or relaxed form, and cooperative binding of oxygen by the four subunits of hemoglobin means that the binding of an oxygen molecule at one heme group increases the oxygen affinity of the remaining heme groups in the same hemoglobin molecule.
- The physiological adaptation to high altitude involves increased tissue concentrations of 2,3-BPG, which lowers the oxygen affinity of hemoglobin, permitting greater unloading of oxygen in the capillaries of the tissues.
- Fetal hemoglobin contains a variant of the β chain, called ɤ (gamma), which has a His→Ser substitution in the 2,3-BPG-binding site, resulting in an enhanced O2-binding affinity that allows transfer of O2 from the maternal to the fetal red blood cells.
- The release of oxygen from hemoglobin is enhanced when the pH is lowered or when the hemoglobin is in the presence of an increased pCO2, a phenomenon known as the Bohr effect.
- Carbon monoxide (CO) binds tightly (but reversibly) to the hemoglobin iron, forming carboxyhemoglobin, which shifts the oxygen dissociation curve to the left and changes the normal sigmoidal shape toward a hyperbola, resulting in the affected hemoglobin being unable to release oxygen to the tissues.
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Description
Test your knowledge of the structure and function of oxygen transport proteins with this quiz! Learn about the essential role of hemoglobin and myoglobin in transporting oxygen, how heme and iron atoms are involved, and the cooperative binding of oxygen by hemoglobin subunits. Explore the oxygen dissociation curve and the effects of physiological adaptations, such as high altitude exposure and fetal hemoglobin. Finally, discover the impact of carbon monoxide on hemoglobin and its ability to release oxygen.
