Table 1 Relative experimental aggregation propensities of the 20 natural amino acids derived from the analysis of mutants in the central position of the CHC in amyloid-β-protein.
From: Prediction of "hot spots" of aggregation in disease-linked polypeptides
Amino acid | Â |
|---|---|
I | 1.822 |
F | 1.754 |
V | 1.594 |
L | 1.380 |
Y | 1.159 |
W | 1.037 |
M | 0.910 |
C | 0.604 |
A | -0.036 |
T | -0.159 |
S | -0.294 |
P | -0.334 |
G | -0.535 |
K | -0.931 |
H | -1.033 |
Q | -1.231 |
R | -1.240 |
N | -1.302 |
E | -1.412 |
D | -1.836 |