Fig. 5: Theoretical and experimental SFG amide-I spectra of InaZ9R at the air–water interface. | Nature Communications

Fig. 5: Theoretical and experimental SFG amide-I spectra of InaZ9R at the air–water interface.

From: Ice-nucleating proteins are activated by low temperatures to control the structure of interfacial water

Fig. 5

A RSS plots illustrating the match between theory and experiment for different tilt (θ) and twist (Ψ) angles. B Calculated spectra resulting from (θ, Ψ) fits starting at the minimum RSS position, resulting in best matching tilt and twist angles of θ = 21° +31°−40° and Ψ = 41° +72°−110° for 20 °C, and θ = 59° +18° −8° and Ψ = 303° +42°−36° for 5 °C (positive and negative uncertainties are given as super- and subscripts, see SI). C Schematic representation of the best matching protein orientations. InaZ9R reorients at lower temperatures, with a more inclined orientation at 5 °C. In a tightly packed protein layer, the low-temperature pose increases the interaction of the INA sites (marked blue) with water.

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