Effects of mutation of A441 on the structural properties of So BADH. Conformational characteristics of wild-type and mutant SoBADH enzymes examined by near- (A) and far-UV (B) CD spectra. (C) Thermal denaturation followed by changes at 222 nm in the far-UV CD signal. The temperature range was 20–90°C and the scan rate 1.5°C/min. The solid lines represent the best fit of the thermal transition data to a sigmoidal Boltzman function by non-linear regression.