For hemoglobin several interactions have been identified to exist in the T state

Question

For hemoglobin several interactions have been identified to exist in the T state, including the ion pairs between Arg (alpha 1)-Asp (alpha 2) and Asp (alpha 1) - Arg (alpha 2) as shown by the figure below. If Arg (alpha 1) is mutated to Ala (alpha 1) or Asp (alpha 2) is mutated to Asn (alpha 2), what would be the impact of these mutations on the O_2 binding curve? Please draw the two curves, one for each mutation, with the O_2 binding curve? Please draw the two curves, one for each mutation, with the O_2 binding curve for wild-type hemoglobin as reference and explain your answer.

Explanation / Answer

The hemoglobin exists in two different states. The T-state which is more tense of the two and is the deoxy form of hemoglobin while the R-state is the relaxed state and is fully oygenated and is also known as oxyhemoglobin. there are three key amino acid residues responsible for the bind of oxygen to the active site: lysine (Lys), histidine (His), and aspartate (Asp).

thus alteration in confermation affect oxygen binding capacity.

Related Questions

Navigate

• Browse (All)
• Browse F
• Subjects

---

---

Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.