Experimentally found Φ-values (larger 0.5) and predicted amyloidogenic regions

Protein or domain nameSizeNumber of residues with known Φ-valuesPredicted amy­loido­genic regionsResidues with experimental Φ-values larger than 0.50 (Φ-value)a
Spliceosomal protein U1A96109–15; 30–45; 53–5944(0.60)
Ribosomal protein S697101–9; 45–516(0.52)
B-domain of staphylococcal protein A 601514–2114(0.65); 17(1.0); 18(1.0); 32(0.57)
Colicin E9 immunity protein861915–22; 34–4013(0.98); 15(0.57); 16(0.52)
Barnase1101987–98; 103–10913(0.60); 15(0.80); 57(1.0); 87(0.80); 90(0.9); 91(1.0); 96(0.40)
Chymotrypsin inhibitor (CI2)643429–35; 39–5218(0.70); 49(0.53)
Ig repeat 27 of titin892256–6423(0.82); 49(0.66); 56(0.52); 58(0.79); 60(0.67); 71(0.63); 75(0.63)
IgG binding domain of streptococcal protein L64387–134(0.51); 7(0.62); 8(0.53); 14(0.85); 21(0.75)
Villin 14T domain 11261818–24; 42–49; 58–6623(0.65); 28(0.58); 44(0.85); 46(0.69); 48(0.62); 73(0.69); 77(0.52); 78(0.56); 81(0.75); 84(0.68)
10th FN3 module of fibronectin941628–35; 69–758(0.55); 34(0.61); 36(0.52); 72(0.51); 74(0.65); 92(0.79)
DNA-binding protein Sso7d641522–26; 30–34b25(0.65); 45(0.59); 57(0.54); 59(0.60)
Barstar892235–565(0.63); 9(0.72); 18(0.69); 25(0.68); 36(0.70); 37(0.59); 50(0.77); 68(0.52); 72(0.81);
Human muscle acylphosphatase981719–25; 91–9811(0.93); 47(0.54); 54(0.98); 94(0.76)
FK-506 binding protein (FKBP12)1072296–10723(0.52); 27(0.85); 63(0.51); 101(0.57)
SH3 domain of src tyrosine kinase transforming protein64269–16; 41–4730(0.62); 32(0.55); 35(0.77); 44(0.54); 47(0.95); 48(0.72); 50(0.86); 53(0.68); 55(0.56); 56(0.71)
Colicin E7 immunity protein871934–443(0.52); 7(0.56); 16(0.72); 18(0.52); 27(0.56); 37(0.51); 44(1.0); 68(0.86); 77(0.86); 78(0.78)
CheY128916–22; 51–57; 80–8635(0.75); 37(0.60); 41(0.68)
IgG binding domain of streptococcal protein G56201–7b32(0.55); 46(0.96); 47(0.67); 49(0.84)
SH3 domain of α-spectrin62138–14; 31–35; 40–44b47(0.63); 52(0.58); 53(0.61); 55(0.53)
3rd Fn3 repeat of tenascin (short form)902519–2636(0.53); 48(0.67); 70(0.54)

aIf several Φ-values are known for a single residue (several different mutations were made), the Φ-values were averaged.

bFor these proteins, amyloidogenic regions are revealed only with window size of five residues. The size of the sliding window for the rest proteins was seven residues.


The fraction of all known experimental Φ-values in the predicted amyloidogenic regions is 25%, the fraction of large Φ-values (>0.5) within amyloidogenic fragments is 33%, such Φ-values are shown bold in Table.

Summary graph


Links:
  • Experimentally measured and theoretically predicted Φ-values
  • The BioInformatics Group site