Fig. 5: Hydrogel formation of different NTs and their thermal stability. | Nature Communications

Fig. 5: Hydrogel formation of different NTs and their thermal stability.

From: Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform

Fig. 5

a Vial inversion tests of NT (100 mg/ml) at pH 8, 7, 6 and with 154 mM NaCl (pH 8) after incubation at 37 °C. b CD spectroscopy of NT with and without 154 mM NaF and 154 mM NaCl, respectively. Molar ellipticity at 222 nm converted to fraction natively folded. c Vial inversion test of NT mutants (100 mg/ml) NT* (37 °C and 60 °C) NTA72R (37 °C) and His-NT-L6 (37 °C and 60 °C). d CD spectroscopy of NT mutants NT*, NTA72R and His-NT-L6. Molar ellipticity at 222 nm converted to fraction natively folded. e Inversion test of NTFlSp, NTMiSp and reduced NTMiSp (100 mg/ml). Scale bars are 5 mm. f CD spectroscopy of NT, NTFlSp, NTMiSp and reduced NTMiSp. Molar ellipticity at 222 nm converted to fraction natively folded. Full spectra of the NTs at 25 °C and 95 °C is shown in Supplementary Fig. 8.

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