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. Author manuscript; available in PMC: 2015 Dec 2.
Published in final edited form as: Phys Chem Chem Phys. 2015 Dec 2;17(48):32149–32160. doi: 10.1039/c5cp03343h

Table 1.

Secondary structures of Aβ1-42, AβpE3-42, and their 1:1 combinations incubated in 50 mM NaCl + 50 mM Na,K-phosphate buffer (shaded rows) or 10 mM Na,K-phosphate buffer, pD 7.2, as determined by curve-fitting of FTIR amide I bands (see Figure S3). Average percentages for 10 min, 1 h, and 2 h incubation in aqueous media are presented. “Other” refers mostly to irregular structure.

1-42 AβpE3-42 1-42 /AβpE3-42 (1:1)
α-helix 11.0±2.4 18.7±3.2 22.9±3.6
24.8±5.1 13.6±1.8 16.3±2.1
β-sheet 50.4±4.6 43.0±4.4 34.5±3.9
38.7±4.8 48.9±3.6 34.2±3.2
β-turn 18.1±3.3 20.3±1.7 28.4±2.4
24.0±2.7 19.8±1.3 27.7±3.6
other 20.5±3.9 18.0±2.2 14.2±1.3
12.5±3.6 17.7±2.6 21.8±2.7