Contribution of the dimeric state to the thermal stability of the flavoprotein D-amino acid oxidase
Protein Sci
Pollegioni et al. 12 (5): 1018.
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Fig. 1S. Effects of heating on the spectra of wild-type (squares) and
delta loop mutant (circles) RgDAAO. Proteins were 0.5 mg/ml in 50 mM
potassium phosphate, pH 7.5, 2 mM EDTA, 10% glycerol. Full symbols,
native; open symbols, heated to 75 degrees C at 0.5 degrees C/min and
cooled to 25 degrees C. For all proteins, spectra recorded at 75
degrees C after progressive heating overlapped those recorded on the previously heated protein after cooling to 25 degrees C. Panel A,
flavin fluorescence. Panel B, tryptophan fluorescence. Panel C,
far-UV circular dichroism.
