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To reveal the contribution of hydrophobic interactions to the stability of the molten globule (MG) state of proteins, the effect of sorbitol on the structure of acid-unfolded (AU) equine heart myoglobin was examined at pH 2 by means of circular dichroism (CD), stopped-flow CD, rheometry, and differential scanning calorimetry. The AU state of myoglobin was refolded by adding sorbitol to the MG state,...
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