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

Ganesh, C and Eswar, Narayanan and Srivastava, Sarika and Ramakrishnan, Chandrasekharan and Varadarajan, Raghavan (1999) Prediction of the maximal stability temperature of monomeric globular proteins solely from amino acid sequence. In: FEBS Letters, 454 (1-2). pp. 31-36.

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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 $(\Delta C_p)$ alone is shown to accurately predict $T_{ms}.\Delta C_p$ 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.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Federation of European Biochemical Societies.
Keywords: Protein;Folding;Stability;Thermodynamics;Heat capacity;Accessible surface area
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 16 Oct 2007
Last Modified: 19 Sep 2010 04:40
URI: http://eprints.iisc.ernet.in/id/eprint/12109

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