Prediction of the maximal stability temperature of monomeric globular proteins solely from amino acid sequence

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Abstract
Globular protein thermostability is characterized the cold denaturation, maximal stability (T ms) and heat denaturation temperatures. For mesophilic globular proteins, T ms typically ranges from −25°C to +35°C. We show that the indirect estimate of T ms from calorimetry and the direct estimate from chemical denaturation performed in a range of temperatures are in close agreement. The heat capacity change of unfolding per mol residue (ΔC p) alone is shown to accurately predict T ms. ΔC p and hence T ms can be predicted solely from the protein sequence. The average difference in free energy of unfolding at the observed and predicted values of T ms is 1.0 kcal mol−1, which is small compared to typical values of the total free energy of unfolding.