Prediction of the maximal stability temperature of monomeric globular proteins solely from amino acid sequence.
Globular protein thermostability is characterized the cold denaturation, maximal stability (Tms) and heat denaturation temperatures. For mesophilic globular proteins, Tms typically ranges from -25 degrees C to +35 degrees C. We show that the indirect estimate of Tms 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 Cp) alone is shown to accurately predict Tms. Delta Cp and hence Tms can be predicted solely from the protein sequence. The average difference in free energy of unfolding at the observed and predicted values of Tms is 1.0 kcal mol(-1), which is small compared to typical values of the total free energy of unfolding.
Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
C
C
Ganesh
N
N
Eswar
S
S
Srivastava
C
C
Ramakrishnan
R
R
Varadarajan
D000465:Algorithms; D000595:Amino Acid Sequence; D016208:Databases, Factual; D019791:Guanidine / Q000494:pharmacology; D008956:Models, Chemical; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013696:Temperature; D013816:Thermodynamics
D011506:Proteins; D019791:Guanidine