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

FEBS Letters

Ganesh, C¹  Ramakrishnan, Chandrasekharan¹  Srivastava, Sarika¹  Eswar, Narayanan¹  Varadarajan, Raghavan¹ 

[1] Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India

关键词: Protein;    Folding;    Stability;    Thermodynamics;    Heat capacity;    Accessible surface area;    ΔA np;    non-polar accessible surface area buried upon folding;    DSC;    differential scanning calorimetry;    N res;    number of residues;    N S-S;    number of disulfide bonds;    T dh;    temperature of heat denaturation;    T ms;    temperature of maximal stability;   

DOI  :  10.1016/S0014-5793(99)00758-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown