Table 4.
Percent of secondary structures of β-crystallinsa
| α-Helix | β-Sheet | β-Turn | Random coil | (other) | |
|---|---|---|---|---|---|
| βA1 | 6 (12)b | 34 (32) | 32 | 28 | (57) |
| βA2c | − (4) | − (39) | - | - | (58) |
| βA3 | 6 (5) | 30 (34) | 34 | 30 | (61) |
| βA4 | 4 (5) | 49 (34) | 19 | 27 | (61) |
| βB1 | 8 (7) | 37 (32) | 23 | 32 | (61) |
| βB2 | 9 (4) | 37 (34) | 26 | 28 | (62) |
| βB3 | 10 (7) | 46 (33) | 18 | 27 | (61) |
a
The content of secondary structures was calculated from CD data by PROSEC program [14].
b
The numbers in the brackets are the secondary structures predicted by PROF program [15]. The program gave only the α-helix and β-sheet; the remaining structures were given as other.
c
Concentration of βA2-crystallin was too dilute for CD measurement.