Fig. 2: Protein thermal stability. | Nature Communications

Fig. 2: Protein thermal stability.

From: Heat stable and intrinsically sterile liquid protein formulations

Fig. 2

a Temperature-dependent CD spectra of the indicated test protein solubilized in PFOc (top row) or PBS (bottom row). Vial graphic utilized in formulation concept images provided by Karon Arnold/Publicdomainpictures.net. b Change in minimum CD ellipticity for each test protein solubilized in PBS (blue) or PFOc (green) at the indicated temperature. Protein identity is identified by the in-register labels at the top of (a). c DSC measured melting temperature (Tm) for each of the indicated test proteins. “>” symbol indicates Tm could not be reached at the highest achievable cell temperature of 100 °C. Bioactivity of β-gal (d), GFP (e), and trypsin (f) in PBS (blue) or PFOc before (25 °C) and after incubation at 90 °C for 30 min. Heat-treated samples are indicated by the thermometer icon. Data shown in (bg) represent the average ± s.d. of n = 3 technical replicates. Statistical significance between conditions is indicated by a line, or in the case of (b) is measured for PBS relative to PFOc at each temperature interval, using one-sided Student’s t-test. Source data for panels a–f are provided as a Source Data file.

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