title: What can we get from varying scan rate in protein differential scanning calorimetry?
abstract: Differential scanning calorimetry has many advantages over other techniques to study the thermal stability of proteins due to its direct measurement of thermodynamic parameters. Most proteins undergo irreversible thermal denaturation causing their thermogram to be scan rate dependent. We modeled reversible and irreversible protein thermograms at varying scan rates. The complete Lumry-Eyring model was used to model the irreversible thermograms at various values of T1/2(temperature at which equilibrium constant equals unity) and T* (temperature at which rate constant equals 1min-1). Our results have shown that the thermal effects of two processes are integrated with decreasing the T* relative to T1/2. It is also shown that the shape of second derivatives of thermograms under different conditions have specific pattern which can be used to judge and estimate the correct model for protein denaturation.
authors.affiliation: Department of Biochemistry, Faculty of Medicine, Ardabil University of Medical Sciences (ArUMS), Daneshgah Street, Ardabil 5618985991, Iran. Electronic address: m.amani@arums.ac.ir.
authors.forename: Mojtaba
authors.initials: M
authors.lastname: Amani
authors.affiliation: Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
authors.forename: Ali A
authors.initials: AA
authors.lastname: Moosavi-Movahedi
authors.affiliation: Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, Russia.
authors.forename: Boris I
authors.initials: BI
authors.lastname: Kurganov
mesh_terms: D002152:Calorimetry, Differential Scanning / Q000379:methods*; D007700:Kinetics; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*; D013696:Temperature
chemical_list: D011506:Proteins
keywords: Differential scanning calorimetry; Irreversible thermal denaturation; Modeling; Scan rate; Second derivative