Surface hydrophobicity and circular dichroism spectroscopy of zebrafish αA-crystallin and three variants.

<p>Indicated in all panels are zebrafish αA-crystallin, V62T, C143S, and T147V variants. (A) Bis-ANS fluorescence spectra at room temperature indicates relative amount of surface hydrophobicity. Excitation wavelength was 390 nm and the protein concentration was 0.1 mg/mL. (B) Far UV CD spectroscopy indicating secondary structure shows a similar abundance of β-sheets in each protein. Scans were performed at 25°C. (C) Near UV CD spectroscopy, with deflections indicating the positions of aromatic amino acids in each tertiary structure. Scans were performed at room temperature.