title: Calculation of the standard molal thermodynamic properties of aqueous biomolecules at elevated temperatures and pressures II. Unfolded proteins.
abstract: Equations of state for completely unfolded proteins have been generated from group additivity algorithms and the revised Helgeson-Kirkham-Flowers (HKF) equations of state to compute the standard molal thermodynamic properties of these molecules at elevated temperatures and pressures. The requisite equations of state parameters were computed from those of groups retrieved by regression of experimental calorimetric and densimetric data reported in the literature. This approach permits calculation of the standard molal thermodynamic properties as a function of temperature and pressure for any completely unfolded protein for which the amino acid sequence is known. Calculations of this kind have been carried out for 11 thermophilic proteins. The thermodynamic properties reported below can be combined with those for protein unfolding to compute the corresponding properties of completely folded (i.e. native) proteins.
authors.affiliation: Department of Earth and Planetary Sciences, Washington University, St. Louis, MO 63130, USA. amend@levee.wustl.edu
authors.forename: J P
authors.initials: JP
authors.lastname: Amend
authors.forename: H C
authors.initials: HC
authors.lastname: Helgeson
mesh_terms: D000465:Algorithms; D002151:Calorimetry; D003574:Cytochrome c Group / Q000737:chemistry; D009113:Muramidase / Q000737:chemistry; D009211:Myoglobin / Q000737:chemistry; D011312:Pressure; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012260:Ribonucleases / Q000737:chemistry; D013696:Temperature; D013816:Thermodynamics
chemical_list: D003574:Cytochrome c Group; D009211:Myoglobin; D011506:Proteins; D012260:Ribonucleases; D009113:Muramidase