Abstract
Caspases are an ancient class of cysteinyl proteases that play an integral part in cell development and apoptosis as an evolutionarily conserved function. During apoptosis, the intracellular pH decreases from 7.4 to ∼ 6.8 and cytosolic acidification affects the activation of caspase-3 and pH-dependent conformational changes affect the rate of auto maturation in the dimeric procaspase-3. This protein folding landscape is sculpted through evolution by selection of stabilizing residues, while repressing the non-native ones.
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