Which of the following best explains why fetal hemoglobin (HbF) has higher affinity for oxygen than HbA? a. HbF binds 2,3-bisphosphoglycerate with lower affinity b. One of the coordination positions of HbF is occupied by an Asp residue c. Oxygen binding is not cooperative in HbF d. The Fe-O bond is shorter in HbF e. The hemes of HbF and HbA have different structures

Which of the following best explains why fetal hemoglobin (HbF) has higher affinity for oxygen than HbA? a. HbF binds 2,3-bisphosphoglycerate with lower affinity b. One of the coordination positions of HbF is occupied by an Asp residue c. Oxygen binding is not cooperative in HbF d. The Fe-O bond is shorter in HbF e. The hemes of HbF and HbA have different structures

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter11: The Blood

Section: Chapter Questions

Problem 1SQE

See similar textbooks

Similar questions

One of the molecules listed below is effective in reducing O2 affinity of human Hb in the absence of BPG: (1) Glucose 6-phosphate (2) Inositol hexaphosphate (3) Maleic acid (4) Lactate (5) Arginine - Interestingly, this molecule plays the role of BPG in bird and turtle hemoglobin. A) Write the chemical structure of each molecule mentioned above. (B) Predict what molecule is most effective in preventing O2 binding to Hb. In 20 words or less explain the rationale for your prediction
Which of the following steps does not occur when the first oxygen molecule binds to HB? a) Heme flattens out b) DPG eventually gets released c) Salt bridges are broken d) Valine 98 forms H-bond with Tyrosine 145
One molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant). (Please provide clear and sufficient explanation for the question, thank you!)
Suppose you mutate the proximal histidine of hemoglobin to glycine. You study the behavior of this mutant hemoglobin in the presence of 10 mM imidazole; the imidazole molecule can substitute for the proximal histidine chain and bind to the heme iron just as histidine does. a) Which state (T or R) will this mutation favor? b) Will oxygen binding to this state be tighter or weaker than oxygen binding to the same state of the wildtype hemoglobin? (note: wildtype means refers to the phenotype of the typical form of a species as it occurs in nature) c) Will this mutant still display significant cooperativity?
Suppose you mutate the proximal histidine of hemoglobin to glycine. You study the behavior of this mutant hemoglobin in the presence of 10 mM imidazole; the imidazole molecule can substitute for the proximal histidine chain and bind to the heme iron just as histidine does. a) Which state (T or R) will this mutation favor? b) Will oxygen binding to this state be tighter or weaker than oxygen binding to the same state of the wildtype hemoglobin? (note: wildtype means refers to the phenotype of the typical form of a species as it occurs in nature) c) Will this mutant still display significant cooperativity (Please provide clear and sufficient explanation for each part, thank you!)
One molecule of 2,3-bisphosphoglycerate (BPG) binds to one molecule of haemoglobin (Hb) in a central cavity of the haemoglobin molecule. Is the interaction between BPG and Hb stronger or weaker than it would be if BPG were bound to the surface of the protein instead? Explain your answer.
To study the chemical properties of the blood hemoglobin of a vertebrate, it might seem convenient to remove the hemoglobin from the red blood cells so that hemoglobin is in simple aqueous solution. However, removing the hemoglobin from red blood cells often promptly alters its O2-binding characteristics. Explain why?
Hemoglobin (Hb) is a blood protein that is responsible for transporting oxygen. It can exist in the protonated form as HbH*. The binding of oxygen can be represented by the simplified equation HbH+ + 02 > ABO2 + Ht A. Excessive vomiting may lead to metabolic alkalosis, in which [H2O*] in blood decreases. How does this condition affect the ability of Hb to transport O2? B.Diabetes mellitus may lead to metabolic acidosis, in which [HgO*] in blood How does this condition affect the ability of Hb to transport O?
The amino acid in Hemoglobin that is most found to be most sensitive to pH changes, and hence affects Oxygen binding process around pH 7 is Valine Tyrosine Histidine Aspartic Acid
How does carbon monoxide affect oxygen transport? A) carbon monoxide binds to the N-terminus forming carbamate B) The presence of carbon monoxide makes hemoglobin work more efficiently C) Carbon monoxide does not affect oxygen transport D) Carbon monoxide stabilizes the R-state E) Carbon monoxide stabilizes the T-state
A mutation in Hb that prevented formation of the tetramer would result in: a A decrease in overall O2 binding affinity but increased O2 transport to muscle. b Increased O2 binding in muscle but decreased binding in lung. c A loss of positive cooperativity and reduced O2 transport efficiency. d All of the above.
A team of biochemists uses genetic engineering to modify the interface region between hemoglobin subunits. The resulting hemoglobin variants exist in solution primarily as αβ dimers (few, if any, α2β2 tetramers form). Are these variants likely to bind oxygen more weakly or more tightly? Explain your answer.