Table 4 |
|||
|
List of the predicted "hot spots" in the different disease-linked polypeptides in this study and comparison with the available experimental data. Experimental "hot spots" refer to those protein regions shown to be involved in the aggregation process of the corresponding polypeptide. It is also noted if the predicted "hot spot" has been described as a structural element of the amyloid fibrils formed by the different peptides and proteins in the study. |
|||
|
Protein |
Predicted "Hot Spots" |
Experimental "Hot Spots" |
Regions in the fibrils |
|
|
|||
|
Amyloid-β-protein |
16–21 |
+ |
+ |
|
30–36 |
+ |
+ |
|
|
38–42 |
+ |
+ |
|
|
Islet amyloid polypeptide |
12–18 |
+ |
uncertain |
|
22–28 |
+ |
uncertain |
|
|
1–18 |
No experimental data available |
uncertain |
|
|
α-Synuclein |
27–56 |
+ |
uncertain |
|
61–94 |
+ |
+ |
|
|
β2-Microgobulin |
21–31 |
+ |
+ |
|
56–69 |
+ |
+ |
|
|
79–85 |
+ |
+ |
|
|
87–91 |
+ |
+ |
|
|
Lysozyme (hen) |
24–34 |
- |
- |
|
50–62 |
+ |
+ |
|
|
76–98 |
+ |
+ |
|
|
Transthyretin |
10–20 |
+ |
+ |
|
23–33 |
No experimetal data available |
uncertain |
|
|
105–118 |
+ |
+ |
|
|
Prion Protein |
1–32 |
No experimetal data available |
uncertain |
|
105–146 |
+ |
+ |
|
|
208–252 |
No experimetal data available |
uncertain |
|
|
|
|||
|
de Groot et al. BMC Structural Biology 2005 5:18 doi:10.1186/1472-6807-5-18 |
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