title: Using a second-order differential model to fit data without baselines in protein isothermal chemical denaturation.
abstract: In vitro protein stability studies are commonly conducted via thermal or chemical denaturation/renaturation of protein. Conventional data analyses on the protein unfolding/(re)folding require well-defined pre- and post-transition baselines to evaluate Gibbs free-energy change associated with the protein unfolding/(re)folding. This evaluation becomes problematic when there is insufficient data for determining the pre- or post-transition baselines. In this study, fitting on such partial data obtained in protein chemical denaturation is established by introducing second-order differential (SOD) analysis to overcome the limitations that the conventional fitting method has. By reducing numbers of the baseline-related fitting parameters, the SOD analysis can successfully fit incomplete chemical denaturation data sets with high agreement to the conventional evaluation on the equivalent completed data, where the conventional fitting fails in analyzing them. This SOD fitting for the abbreviated isothermal chemical denaturation further fulfills data analysis methods on the insufficient data sets conducted in the two prevalent protein stability studies.
authors.affiliation: Key Laboratory of Cell Proliferation and Regulation of Ministry of Education, Beijing Normal University, Beijing, 100875, China.
authors.forename: Chuanning
authors.initials: C
authors.lastname: Tang
authors.affiliation: Neotein Therapeutics, New York, New York, 10706, USA.
authors.forename: Scott
authors.initials: S
authors.lastname: Lew
authors.affiliation: Key Laboratory of Cell Proliferation and Regulation of Ministry of Education, Beijing Normal University, Beijing, 100875, China.
authors.forename: Dacheng
authors.initials: D
authors.lastname: He
mesh_terms: D002152:Calorimetry, Differential Scanning; D008956:Models, Chemical; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D011506:Proteins
keywords: baselines-missing; chemical denaturation; protein unfolding; second-order derivative data analysis