Figure 7
From: Exploration of Protein Unfolding by Modelling Calorimetry Data from Reheating
The complex three-step modelling of thermal unfolding of wild type DhaA. (A) DSC data (black) for the denaturation of DhaA wild type: first runs (circles), reheated runs for terminal temperatures 49, 51, 54, 61, and 69 °C (not shown), fitted curves for the first run (blue) with decomposition by peaks (dotted) from model C plus one negative peak at high temperatures. (B) Respective modelled fractions of states for a given temperature: native folded (black), first intermediate (yellow), second intermediate (brown) and denatured (red) states. The scan rate was 1 °C min−1.
