Group additivity schemes for the calculation of the partial molar heat capacities and volumes of unfolded proteins in aqueous solution.
A critical review is given of the present state of group additivity schemes for the calculation of partial molar volumes and heat capacities of unfolded proteins. The comparison between the experimental values and the predictions based on the different models shows clearly that only the peptide-based additivity scheme represents properly both the absolute values and the temperature dependence of these thermodynamic quantities.
Hedwig
Gavin R
GR
Institute of Fundamental Sciences-Chemistry, Massey University, Private Bag 11222, Palmerston North, New Zealand. g.hedwig@massey.ac.nz
Hinz
Hans-Jürgen
HJ
D000465:Algorithms; D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D005998:Glycine / Q000737:chemistry; D006801:Humans; D008956:Models, Chemical; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012996:Solutions; D013696:Temperature; D013816:Thermodynamics; D014867:Water
D000596:Amino Acids; D011506:Proteins; D012996:Solutions; D014867:Water; D005998:Glycine