Possibility for discriminating between two representative non two-state thermal unfolding models of proteins by DSC.
Possible differences between two representative non two-state thermal unfolding mechanisms of protein are discussed concerning differential scanning calorimetry. Numerical simulations showed that, by DSC measurement, it is hard to discriminate between the independent model, which assumes independent unfolding domains in a protein, and the sequential model, which assumes intermediate(s) between native and denatured states, especially when values of molecular weight, denaturation enthalpy, and difference in denaturation temperature of each denaturation process are large. DSC curve analysis of Aspergillus niger glucoamylase based on these two models gave essentially the same thermodynamic parameters.
Tanaka
A
A
Faculty of Bioresources, Mie University, Japan. akiyoshi@bio.mie-u.ac.jp
Kobayashi
D
D
Senoo
K
K
Obata
H
H
D001234:Aspergillus niger / Q000201:enzymology; D002152:Calorimetry, Differential Scanning; D003198:Computer Simulation; D005087:Glucan 1,4-alpha-Glucosidase / Q000737:chemistry; D006358:Hot Temperature; D008956:Models, Chemical; D011487:Protein Conformation; D017510:Protein Folding
D005087:Glucan 1,4-alpha-Glucosidase