Evaluation of thermodynamic properties of irreversible protein thermal unfolding measured by DSC |
| |
| Authors: | G D Manetto C La Rosa D M Grasso D Milardi |
| |
| Institution: | (1) Dipartimento di Scienze Chimiche, Universitá di Catania, Viale Andrea Doria 6, 95125 Catania, Italy;(2) Dipartimento di Scienze Chimiche, Università di Catania, Viale Andrea Doria 6, 95125 Catania, Italy;(3) Dipartimento di Scienze Chimiche, Università di Catania, Viale Andrea Doria 6, 95125 Catania, Italy;(4) CNR, Istituto di Biostrutture e Bioimmagini, Sezione di Catania, Viale Andrea Doria 6, 95125 Catania, Italy |
| |
| Abstract: | Summary We assessed the applicability of the extrapolation procedure at infinite scanning rate to differential scanning calorimetry (DSC) data related to irreversible protein unfolding. To this aim, an array of DSC curves have been simulated on the basis of the Lumry-Eyring model N↔U→F. The results obtained confirmed that when the apparent equilibrium constant Kapp (T=T1/2) is lower than 3, the application of the extrapolation procedure provides accurate thermodynamic parameters. Although this procedure applies only to monomeric proteins for which the Lumry-Eyring model is a reasonable approximation, it will hopefully contribute to increase the potential of DSC in obtaining reliable thermodynamic information regarding the folding/unfolding equilibrium. |
| |
| Keywords: | differential scanning calorimetry reliability extrapolation to infinite scan rate |
| 本文献已被 SpringerLink 等数据库收录！ |
|
