Thermodynamic model for the analysis of calorimetric data of oligomeric proteins

M.I. BURGOS; S.A. DASSIE; G.D. FIDELIO

American Chemical Society

Lugar: New York; Año: 2008 vol. 112 p. 14325 - 14325

font face="Times-Roman" size="2"> The thermodynamic parameters for the process of protein unfolding can be obtained through differential scanning calorimetry. However, the unfolding process may not be a two-state one. Between the native and the unfolded state, there may be association or dissociation processes or the formation of an intermediate state. As a consequence of this, the precise interpretation of the calorimetric data should be done with a specific thermodynamic model. In this work, we present two general models for the unfolding process of an oligomeric protein: Nn h nN h n