Table 1.

Comparison of Important Secondary Structures Present in the Aβ42 and MTSL-Cys-Aβ42 Ensemble

Sequence Region	Secondary Structure %	Aβ42	MTSL-Cys-Aβ42
Localized secondary structure (helices and turns) for N-terminal residues 1–15	turn 1–2/turn 2–3∗	4.4 ± 1.5∗	23.3 ± 2.3∗
	turn 3–4/turn 5–6	7.6 ± 5.3	10.0 ± 5.0
	turn 7–8/turn 8–9	36.0 ± 17.4	32.6 ± 25.0
	turn 9–10/turn 10–11	14.4 ± 4.7	15.6 ± 0.2
	turn 11–12	7.4 ± 4.0	7.4 ± 1.1
	turn 12–13/turn 13–14	12.2 ± 1.2	12.6 ± 4.7
	turn/helix 14–15	24.4 ± 11.4	9.3 ± 3.4
	turn 17–18	3.6 ± 0.6	12.8 ± 13.8
	turn 21–22/turn 22–23	5.0 ± 2.7	11.6 ± 2.5
Localized secondary structure (helices and turns) for central residues 16–30	turn 23–24/turn 24–25	10.7 ± 2.0	22.8 ± 9.5
	turn/helix 25–26	21.0 ± 4.4	21.2 ± 15.7
	turn/helix 26–27	22.8 ± 4.7	12.8 ± 4.4
	turn 29–30	10.8 ± 5.0	4.6 ± 2.4
Localized secondary structure (helices and turns) for C-terminal residues 31–42	turn 30–31/turn 31–32∗	15.8 ± 1.6∗	3.8 ± 0.2∗
	turn 32–33∗	7.3 ± 1.3∗	45.6 ± 1.6∗
	turn 33–34∗	9.3 ± 1.8∗	3.2 ± 2.2∗
	helix 32–33/helix 33–34	6.8 ± 1.1	12.3 ± 8.1
	helix 34–35	6.4 ± 1.9	8.4 ± 0.8
	helix 35–36	3.2 ± 1.1	6.1 ± 0.6
	turn 36–37	6.6 ± 0.5	5.2 ± 0.1
Residues involved in β-strand pairings	turn 37–38	6.6 ± 1.9	9.3 ± 6.7
	β-strands 3–6 and 31–41	0.5 ± 0.7	6.6 ± 8.6
	β-strands 16–21 and 29–36	8.7 ± 6.6	17.8 ± 13.8
	β-strands 27–31 and 33–38∗	5.0 ± 4.3∗	38.0 ± 6.9∗
	β-strands 34–36 and 39–40	2.2 ± 1.5	5.4 ± 6.8

The asterisks indicate the structural features whose populations differ in the untagged and tagged ensembles by a larger standard deviation than that observed for REMD and TCW ensembles of the Aβ42 ensemble.