Table 1 Amide I wavenumbers (ν), fractions (f), and numbers of amino acid residues (N) for α-helix, β-sheet, unordered (ρ) structures, and turn and “other” structures (other), derived from ATR-FTIR spectra

From: The structure of tyrosine-10 favors ionic conductance of Alzheimer’s disease-associated full-length amyloid-β channels

 

Aβ1-42

Aβ1-40

AβpE3-42

AβpE3-40

να(cm−1)

1659–1657a

1656–1654

1651–1646

1666–1663b

1652-1651

1668-1666b

fα

0.194 ± 0.0236

0.153 ± 0.0170

0.254 ± 0.0548

0.088 ± 0.0401b

0.212 ± 0.0396

0.121 ± 0.0421b

Nα

8.15 ± 0.992

6.12 ± 0.680

10.16 ± 2.193

3.52 ± 1.606b

8.06 ± 1.504

4.60 ± 1.600b

νβ(cm−1)

1627

1629

1628

1627–1625

fβ

0.459 ± 0.0367

0.170 ± 0.0190

0.351 ± 0.0521

0.270 ± 0.0419

Nβ

19.27 ± 1.541

6.80 ± 0.760

14.04 ± 2.0846

10.27 ± 1.591

νρ(cm−1)

1643–1642

1642–1640

1641–1637

1639–1637

fρ

0.188 ± 0.0150

0.140 ± 0.0525

0.065 ± 0.0596

0.176 ± 0.0809

Nρ

7.90 ± 0.626

5.60 ± 2.100

2.60 ± 2.383

6.70 ± 3.0747

νother(cm−1)

1700–1678

1705-1669

1699-1678

1700-1681

fother

0.159 ± 0.0151

0.537 ± 0.0551

0.242 ± 0.0549

0.221 ± 0.0405

Nother

6.68 ± 0.632

21.48 ± 2.204

9.68 ± 2.197

8.37 ± 1.539

  1. The range of wavenumbers and mean  ±  standard deviation values have been determined from three independent experiments.
  2. aWavenumbers of ⊥ spectra are usually slightly lower than those of ǁ spectra.
  3. bThese components have been assigned to αII-helix, although β-turn structure is also possible.
Back to article page