title: Heat capacity change for ribonuclease A folding.
abstract: The change in heat capacity deltaCp for the folding of ribonuclease A was determined using differential scanning calorimetry and thermal denaturation curves. The methods gave equivalent results, deltaCp = 1.15+/-0.08 kcal mol(-1) K(-1). Estimates of the conformational stability of ribonuclease A based on these results from thermal unfolding are in good agreement with estimates from urea unfolding analyzed using the linear extrapolation method.
authors.affiliation: Department of Medical Biochemistry and Genetics, Texas A&M University, College Station 77843-1114, USA. nickpace@tamu.edu
authors.forename: C N
authors.initials: CN
authors.lastname: Pace
authors.forename: G R
authors.initials: GR
authors.lastname: Grimsley
authors.forename: S T
authors.initials: ST
authors.lastname: Thomas
authors.forename: G I
authors.initials: GI
authors.lastname: Makhatadze
mesh_terms: D002152:Calorimetry, Differential Scanning; D006358:Hot Temperature; D011489:Protein Denaturation; D017510:Protein Folding; D012259:Ribonuclease, Pancreatic / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D012259:Ribonuclease, Pancreatic