Figure 5 of Murugesan, Mol Vis 2008; 14:1835-1844.


Figure 5. Bis-ANS binding and intrinsic tryptophan fluorescence profile of mutant αBI5C and αBT162C proteins. A: Bis-ANS 10 μl (1 mM) was added to protein samples of 0.2 mg/ml in 50 mM phosphate buffer (pH.7.2) were excited at 385 nm, and emission was scanned between 400 nm and 600 nm. The mutant αBI5C and αBT162C proteins show similar bis-ANS intensity like wild-type αB-crystallin. B: The intrinsic tryptophan fluorescence spectra of wild-type αB-crystallin, αBI5C and αBT162C. Protein samples (0.2 mg/ml) in 50 mM phosphate buffer (pH 7.2 ) were used. The samples were excited at 295 nm and the emission was scanned between 310 nm and 400 nm. Tryptophan spectrum of mutant αBI5C and αBT162C proteins were comparable to the wild-type αB-crystallin spectrum. The data suggests that the mutation did not alter the native conformations of mutant proteins under reducing conditions.