Table 2.

The structural conformation ratios in silk fibroin scaffolds derived from deconvoluted amide I FTIR spectra.

Samplesa	Conformation content of silk fibroin
	Random	β-Sheet	Silk I (Type II β-turn)	Bends and Turns
SS-0	40.7 ± 3.4	16.6 ±1.7	13.9± 1.6	27.5 ± 2.8
SS-2	35.4 ± 3.2	20.3 ± 1.8	14.7 ± 1.8	27.0 ± 2.6
SS-6.3	30.3 ± 3.1	24.9 ± 2.7	16.5 ± 1.9	25.9 ± 2.4
SS-11.8	26.3 ± 2.0	28.3 ± 2.6	18.7 ± 1.9	23.4 ± 2.3
SS-33.3	22.9 ± 2.2	32.3 ± 3.1	20.1 ± 2.0	21.2 ± 2.1
SS-6.3b	16.4 ± 1.7	38.8 ± 2.1	26.6 ± 2.1	16.2 ± 1.8
SS-11.8b	15.2 ± 1.8	42.5 ± 2.4	21.4 ± 2.3	17.4 ± 1.6
SS-33.3b	15.4 ± 1.4	46.9 ± 3.3	17.4 ± 1.9	16.8 ± 1.8

^aTen measurements per condition were obtained.

^bWater-insoluble silk nanofibrous scaffolds.