Table 2.
Fold change in mass, secondary structure, tertiary structure and chaperone activity in αA-crystallin mutants as compared to αA-wt
| αA-samples | Average Molar Massa | Secondary Structureb | Tertiary Structurec | Chaperone activityd |
|---|---|---|---|---|
|
| ||||
| αA-wt | 1.00 | 1.00 | 1.00 | 1.00 |
| αA-R12C | 2.10 | 3.00 | 2.00 | 0.60 |
| αA-R21L | 0.90 | 4.10 | 1.00 | 0.80 |
| αA-R21W | 1.20 | 6.20 | 3.10 | 0.60 |
| αA-R49C | 0.90 | 2.00 | 1.00 | 1.00 |
| αA-R54C | 1.40 | 3.00 | 3.20 | 0.90 |
| αA-R116C | 5.10 | 4.30 | 4.00 | 0.10 |
| αA-R116H | 7.00 | 5.20 | 5.00 | 0.30 |
a
Average molar mass values from Table 1 were used
b
Molar ellipticity values at around 195 nm from Fig. 4 indicative of α-helix content were used
c
Molar ellipticity values at around 293 nm (Trp signals) and at around 285 nm (Tyr/Trp Signals) from Fig. 5 were used
d
Chaperone activity assay values from Fig. 9b were used