Figure 3 | Scientific Reports

Figure 3

From: Engineered ice-binding protein (FfIBP) shows increased stability and resistance to thermal and chemical denaturation compared to the wildtype

Figure 3

Thermal stability of mutants and thermal hysteresis (TH) activity of FfIBP_WT and FfIBP_CC1. (a) Melting temperature of FfIBP, FfIBP_CC1, FfIBP_CC2, FfIBP_CC3, and FfIBP_CC4 without chemicals. (b) Burst ice crystal morphology in a solution of 20 µM FfIBP and FfIBP_CC1. Ice crystals were grown after the temperature exceeded the TH gap. (c) Concentration-dependent TH activity of FfIBP and FfIBP_CC1. All the measurements were performed in triplicate and averaged.

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