Amani Mojtaba, Moosavi-Movahedi Ali A, Kurganov Boris I
Department of Biochemistry, Faculty of Medicine, Ardabil University of Medical Sciences (ArUMS), Daneshgah Street, Ardabil 5618985991, Iran.
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
Int J Biol Macromol. 2017 Jun;99:151-159. doi: 10.1016/j.ijbiomac.2017.02.010. Epub 2017 Feb 11.
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 T (temperature at which equilibrium constant equals unity) and T* (temperature at which rate constant equals 1min). Our results have shown that the thermal effects of two processes are integrated with decreasing the T* relative to T. 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.
