Protein Stability─Analysis of Heat and Cold Denaturation without and with Unfolding Models.

ABSTRACT: Protein stability is important in many areas of life sciences. Thermal protein unfolding is investigated extensively with various spectroscopic techniques. The extraction of thermodynamic properties from these measurements requires the application of models. Differential scanning calorimetry (DSC) is less common, but is unique as it measures directly a thermodynamic property, that is, the heat capacity C_p(T). The analysis of C_p(T) is usually performed with the chemical equilibrium two-state model. This is not necessary and leads to incorrect thermodynamic consequences. Here we demonstrate a straightforward model-independent evaluation of heat capacity experiments in terms of protein unfolding enthalpy ΔH(T), entropy ΔS(

SUBMITTER: Seelig J 

PROVIDER: S-EPMC10123674 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature