Table 1.

Secondary structure content of eADF assemblies

Protein assembly	Structure composition, %
	Helical(1648–1664 cm−1)	β-Sheet (1625–1640 and1688–1692 cm−1)	β-Turn(1665–1685 cm−1)
eADF3	55	18	16
eADF3 fiber	31	45	25
eADF4 with phosphate	16	63	21
eADF3 + eADF4 fiber	46	40	13

Infrared spectra were analyzed to determine secondary structure composition of the protein assemblies. eADF3 assemblies generally showed more helical structures than eADF4 assemblies, which revealed a high content of β -sheet structures. Fibers of eADF3 and eADF4 showed β -sheet-rich secondary structure (peak at 1,625 cm⁻¹). However, eADF3 fibers revealed a higher relative content of β -sheet structures than the mixed fibers of eADF3 and eADF4. Details of the structure assignment can be found in Fig. S2. Deviations from 100% result from unassigned spectral regions and from rounding errors.