Figure 7. Structural changes in sodium deoxycholate-treated, 25 kDa βA3-crystallin species with proteinase activity compared to untreated, 32 kDa WT βA3-crystallin without enzyme activity. These preparations were obtained as described in Figure 6. A: The far UV-CD spectra show that the truncated 25 kDa βA3-species (red line) contains a greater level of alpha helical content than the WT-βA3 (black line). B: The intrinsic Trp fluorescence spectra show a red shift in the truncated 25 kDa βA3-species (red line) as compared to the WT-βA3 (black line). C: The fluorescence spectra after ANS-binding show a blue shift in the truncated 25 kDa βA3-species (red line) as compared to the WT-βA3 (black line).