What would be the expected result of a lysine residue being substituted with a serine residue in the BPG binding site of hemoglobin?

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Quizplus · Accepted Answer

Lysine is a positively charged amino acid, and it plays a crucial role in the binding of BPG to hemoglobin. The positively charged lysine residues interact with the negatively charged BPG molecules, stabilizing their binding. If a lysine residue is substituted with a serine residue, the positive charge would be lost, and the interaction between BPG and hemoglobin would be weakened, resulting in weaker binding. Therefore, BPG would bind less tightly because of the loss of a positive charge.

What Would Be the Expected Result of a Lysine Residue