Figure 2
Figure 2. Thermal denaturation analysis of α0-1 recombinant peptides. Representative thermal denaturation experiments of wild-type and 2 HE mutant α0-1 peptides. DSC analysis was performed at a scan rate of 90°C/hr in 10 mM sodium phosphate, 130 mM NaCl, 1 mM β-ME, pH 7.4, at concentrations ranging from 0.6 to 1.0 mg/mL. Normalized spectra are shown for: the α0-1 wild-type (—), Tm = 54.6°C; the α0-1 R28C (···), which had the highest observed Tm of 55.6°C; and the α0-1 R34W (----), which had the lowest Tm at 49.1°C and the most atypical melting curve.

Thermal denaturation analysis of α0-1 recombinant peptides. Representative thermal denaturation experiments of wild-type and 2 HE mutant α0-1 peptides. DSC analysis was performed at a scan rate of 90°C/hr in 10 mM sodium phosphate, 130 mM NaCl, 1 mM β-ME, pH 7.4, at concentrations ranging from 0.6 to 1.0 mg/mL. Normalized spectra are shown for: the α0-1 wild-type (—), Tm = 54.6°C; the α0-1 R28C (···), which had the highest observed Tm of 55.6°C; and the α0-1 R34W (----), which had the lowest Tm at 49.1°C and the most atypical melting curve.

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