HbS, the variant of hemoglobin responsible for sickle-cellanemia, aggregates into long chains in aqueous, biologicalconditions (pH 7.4, 37oC, some salt and bufferpresent).
Explain this phenomenon from a molecular point of view. Why doesit form chains, not globular aggregates?
Why is this phenomenon unsurprising to biochemists familiar withthe details of protein folding?
