Table III.
Summary of Secondary Structure and Solvent Accessibilitiesa
| Amyloidogenic sequences | Non-amyloidogenic sequences | ||
|---|---|---|---|
| Hydrogen-bonds per residueb | 1.12 | 1.03 | |
| Accessible surface area per residue (relative) %c | 25.6 | 26.5 | |
| Secondary structure distributiond % | Helix | 34.5 | 30.7 |
| Strand | 36.0 | 29.4 | |
| Coil | 29.5 | 39.9 | |
1
Values for each characteristic in individual proteins were summed and expressed as an average of the total of 577 amyloidogenic residues and 15,659 non-amyloidogenic residues (16,236 amino acid residues in toto).
2
Number of hydrogen-bonds per residue estimated by VADAR.83 In the case of the 20S proteasome, only chains N and 2 containing the amyloidogenic sequence and chains interacting through hydrogen-bonds with these were included in the analysis.
3
Accessible surface area, average relative surface area per residue (%) computed by the NACCESS program.91
4
Secondary structure distribution (%) according to DeepView: Swiss-PdbViewer.102