Thermal denaturation of RIα(92–381) monitored by far-UV CD.

<p>A) Selected far-UV CD spectra of apo (solid line) and cAMP-saturated (10 fold-molar excess of cAMP; dashed line) RIα(92–381), at 25°C (black), 45°C (red), 69°C (green) and 85°C (blue). B) CD spectra of apo-RIα(92–381) were recorded every 4°C over the temperature interval 25–95°C at a scan rate of 2°C/min, with 4 scans at each temperature (100 nm/min). N indicates the native and F the final (irreversible) states. C) Temperature dependence of CD signal at 216 nm in the apo (○) and cAMP-saturated states (•). All experiments were performed at a protein concentration of 2 µM.