Facilitated Cross-Bridge Interactions with Thin Filaments by Familial Hypertrophic Cardiomyopathy Mutations in α-Tropomyosin

Table 2

Estimates of structural content of WT and mutant tropomyosins.

	α-helix (%)		β-sheet (%)	β-turn (%)	Unordered (%)
	[θ]222	CDPro	CDPro	CDPro	CDPro
α-GS-Tm WT	84.5±4.6	79.1±10.8	4.3±3.4	7.0±6.7	10.4±5.8
α-GS-Tm V95A	60.6±10.4	62.7±6.4	8.2±3.2	12.2±3.5	17.0±5.1
α-GS-Tm D175N	72.1±0.7	72.9±7.0	5.6±3.7	11.3±5.5	13.3±6.0
α-GS-Tm E180G	69.7±3.3	67.9±5.6	5.9±2.7	9.5±4.7	17.3±3.7
β-GS-Tm WT	83.6±6.4	77.8±13.1	5.2±4.4	7.8±6.5	10.1±8.8

Estimates of structural content for each of the five recombinant Tm’s were obtained from analyses of the individual CD spectra that were averaged for Figure 4. α-helical content was estimated from [θ]₂₂₂ (Methods). Content of α-helix, β-sheet, and unordered structure was obtained using CDPro software (Methods). Values are mean ± S.D. (𝑁=2-3 spectra); note that, for CDPro estimates, S.D. is the mean of S.D. values from CDPro.