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HbS, the variant of hemoglobin responsible for sickle-cell anemia, aggregates into long chains in aqueous, biological conditions...

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Biology

HbS, the variant of hemoglobin responsible for sickle-cellanemia, aggregates into long chains in aqueous, biologicalconditions (pH 7.4, 37oC, some salt and bufferpresent).

  1. Explain this phenomenon from a molecular point of view. Why doesit form chains, not globular aggregates?

  2. Why is this phenomenon unsurprising to biochemists familiar withthe details of protein folding?

Answer & Explanation Solved by verified expert
3.5 Ratings (621 Votes)
Normal hemoglobin Hb is made up of 2 alpha subunits and 2 beta subunits In sickle hemoglobin HbS a missense mutation results in substitution of glutamicacid acid a hydrophilic amino acid with valine a hydrophobic amino acid on the surface of HbS in the sixth    See Answer
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