Before revision:  The appearance of the unfolded intermediate occurs at a higher temperature in nCaM than it does in cCaM . That is, we find that cCaM unfolds more readily along the transition route than nCaM. Furthermore, unfolding and refolding of the domain significantly slows the domain opening and closing rates of cCaM , a distinct scenario which can potentially influence the mechanism of calcium binding to each domain.
After revision:  The appearance of the unfolded intermediate occurs at a higher temperature in nCaM than it does in cCaM consistent with nCaM's higher thermal stability. Under approximate physiological conditions, the simulated unfolded state population of cCaM accounts for 10\% of the population with nearly all of the sampled transitions (approximately 95\%) unfolding and refolding of the domain significantly slows the domain opening and closing rates of cCaM , a distinct scenario which can potentially influence the mechanism of calcium binding to each domain.