Property | Amyloid | Non-amyloid | Difference |
|---|
K
0
| -31.966 | -31.675 | -0.291 |
H
t
| 1.693 | 1.546 | 0.147 |
H
p
| 13.461 | 13.001 | 0.460 |
P
| 6.535 | 12.132 | -5.597 |
pH i | 5.801 | 5.997 | -0.196 |
pK' | 2.004 | 2.046 | -0.042 |
M w | 134.369 | 135.217 | -0.848 |
B
l
| 17.329 | 16.377 | 0.952 |
R
f
| 12.353 | 11.152 | 1.202 |
μ | 18.155 | 18.051 | 0.104 |
H
nc
| 0.497 | 0.264 | 0.233 |
E
sm
| 1.207 | 1.201 | 0.006 |
E
l
| 0.608 | 0.563 | 0.044 |
E
t
| 1.817 | 1.767 | 0.050 |
P
α
| 1.032 | 1.050 | -0.018 |
P
β
| 1.231 | 1.088 | 0.143 |
P
t
| 0.817 | 0.879 | -0.062 |
P
c
| 0.875 | 0.926 | -0.051 |
C
a
| 34.890 | 34.666 | 0.224 |
F | 0.895 | 0.934 | -0.039 |
B
r
| 0.369 | 0.321 | 0.048 |
R
a
| 4.998 | 4.409 | 0.589 |
N
s
| 6.544 | 6.250 | 0.294 |
αN | 1.111 | 1.079 | 0.032 |
αC | 0.929 | 1.030 | -0.101 |
αm | 0.968 | 0.990 | -0.022 |
V0 | 95.343 | 94.341 | 1.002 |
N
m
| 1.818 | 1.848 | -0.030 |
N
l
| 4.497 | 4.179 | 0.318 |
H
gm
| 13.845 | 13.459 | 0.386 |
ASA
D
| 156.030 | 156.043 | -0.013 |
ASA
N
| 43.340 | 49.795 | -6.455 |
ΔASA | 112.345 | 105.918 | 6.427 |
ΔGh | -1.662 | -1.903 | 0.241 |
GhD | -2.864 | -3.460 | 0.596 |
GhN | -1.172 | -1.455 | 0.283 |
ΔHh | -4.896 | -4.964 | 0.067 |
-TΔSh | 3.235 | 3.061 | 0.174 |
ΔCph | 25.269 | 22.474 | 2.796 |
ΔGc | 1.854 | 2.074 | -0.220 |
ΔHc | 5.833 | 5.733 | 0.100 |
-T ΔSc | -3.983 | -3.663 | -0.321 |
Δ
G
| 0.190 | 0.170 | 0.020 |
Δ
H
| 0.934 | 0.766 | 0.168 |
-TΔS | -0.744 | -0.597 | -0.147 |
v | 4.253 | 4.314 | -0.061 |
s | 1.382 | 1.460 | -0.078 |
f | 1.788 | 1.916 | -0.128 |
Pϕ-ψ | 0.817 | 0.955 | -0.138 |
- Abbre viations: K0, compressibility; Ht, thermodynamic transfer hydrophobicity; Hp, surrounding hydrophobicity; P, polarity; pH i, isoelectric point; pK':equilibrium constant with reference to the ionization property of COOH group; Mw, molecular weight; Bl , bulkiness; Rf, chromatographic index; β,refractive index; Hnc , normalized consensus hydrophobicity; Esm, short and medium range non-bonded energy; El , long-range non-bonded energy; Et, total non-bonded energy; Pα, Pβ, Pt and Pc are, respectively, β-helical, β-structure, turn and coil tendencies; Ca, helical contact area; F, mean rms fluctuational displacement; Br, buriedness; Ra, solvent accessible reduction ratio; Ns , average number of surrounding residues; βN, βC and βm are, respectively, power to be at the N-terminal, C-terminal and middle of β-helix; V0, partial-specific volume; Nm and Nl are, respectively, average medium and long-range contacts; Hgm, combined surrounding hydrophobicity (globular and membrane); ASAD, ASAN and βASA are, respectively, solvent accessible surface area for denatured, native and unfolding; βGh , GhD and GhN are, respectively, Gibbs free energy change of hydration for unfolding, denatured and native protein; βHh, unfolding enthalpy change of hydration; -T βSh, unfolding entropy change of hydration; βCph , unfolding hydration heat capacity change; βGc , βHc and -T βSc are, respectively, unfolding Gibbs free energy, unfolding enthalpy and unfolding entropy changes of chain; βG, βH and -T βS are, respectively, unfolding Gibbs free energy change, unfolding enthalpy change and unfolding entropy change; v, volume (number of non-hydrogen side chain atoms); s, shape (position of branch point in a side-chain); f, flexibility (number of side-chain dihedral angles); Pϕ-ψ: backbone dihedral probability.
