Question 1
Which molecule serves as a positive allosteric regulator of hemoglobin?
Question 2
What is the structural difference between myoglobin and hemoglobin?
Question 3
How does 2,3-Bisphosphoglycerate (2,3-BPG) affect hemoglobin?
Question 4
What is the functional role of myoglobin in tissues?
Question 5
What is the primary function of hemoglobin in the blood?
Question 6
Which aspect of hemoglobin structure allows for positive cooperativity?
Question 7
What molecule forms when carbon monoxide binds to hemoglobin?
Question 8
What is the Bohr effect regarding hemoglobin's oxygen affinity?
Question 9
What is the main difference in oxygen affinity between myoglobin and hemoglobin?
Question 10
Which protein has a sigmoidal oxygen binding curve?
Question 11
Which histidine residue in the heme group stabilizes the bound oxygen?
Question 12
How does fetal hemoglobin differ from adult hemoglobin in terms of 2,3-BPG?
Question 13
What causes hemoglobin to shift from the T (Tense) to the R (Relaxed) form?
Question 14
In which form does hemoglobin have a higher affinity for oxygen?
Question 15
Which structure is responsible for hemoglobin's oxygen-binding capacity?