. 2014 Dec 8;141(22):225101. doi: 10.1063/1.4902229

Table II.

Protein secondary structure at τ for Aβ₄₀ and Aβ₄₂ in PC or PC/CHOL bilayers.

Aβ in lipid	Replicate	τ^a (ns)	n_H(τ) in the non-LID^b	θ_H(τ) in the non-LID^c	n_H(τ) in the LID^b	θ_H(τ) in the LID^c
Aβ₄₀ in PC	A0		13	1	9	1
	A1	0.20	13.0 ± 0.00	1.00 ± 0.00	8.09 ± 0.16	0.89 ± 0.02
Aβ₄₂ in PC	B0		15	1	10	1
	B1	0.17	15.0 ± 0.00	1.00 ± 0.00	9.36 ± 0.24	0.94 ± 0.02
	B2	9.76	12.5 ± 0.39	0.83 ± 0.03	2.25 ± 0.39	0.26 ± 0.04
Aβ₄₀ in PC/CHOL	C0		13	1	9	1
	C1	3.49	11.5 ± 0.37	0.88 ± 0.03	6.73 ± 0.33	0.75 ± 0.04
	C2	7.57	12.7 ± 0.27	0.98 ± 0.02	5.91 ± 0.16	0.66 ± 0.02
Aβ₄₂ in PC/CHOL	D0		15	1	10	1
	D1	4.89	14.8 ± 0.12	0.99 ± 0.01	9.82 ± 0.12	0.98 ± 0.01
	D2	1.90	12.0 ± 0.47	0.80 ± 0.03	6.50 ± 0.37	0.65 ± 0.04
	D3	17.8	16.8 ± 0.18	1.12 ± 0.01	2.73 ± 0.14	0.27 ± 0.01
	D4	1.04	15.0 ± 0.07	1.00 ± 0.01	8.67 ± 0.29	0.87 ± 0.03

^{^a}

τ, the half-time for the C-terminus to diffuse from its initial location to its anchor site is found from Aβ from the sigmoidal fit (Eq. (1) or Eq. (2)).

^{^b}

Number of helices (n_H(τ)) in the non-LID (Asp-1 to Asn-27) or LID region (Lys-28 to C-terminus) of Aβ at τ.

^{^c}

Fractional helical content (θ_H(τ) = n_H(τ)/ n_H(0)) in the non-LID or LID region of Aβ at τ. Here n_H(0) is the initial number of helices before the simulations as given by the number listed in the A0-D0 row. All n_H calculations (mean ± SE) were from the DSSP analysis averaged over the 100 ps centered at τ.