Effect of the SNP mutations on the enzyme structure: Trp (A) and ANS (B) Fluorescence spectra.

<p>CKs were dissolved in 20 mM Tris-HCl buffer, pH 8.0, with a final concentration of 0.2 mg/ml. Intrinsic fluorescence spectra were recorded using an excitation wavelength of 295 nm and an emission wavelength range of 300–400 nm. ANS fluorescence spectra were obtained by adding a 60-fold molar excess of ANS to the samples, which were then incubated for 30 min in the dark and then recorded from 400–600 nm. All experiments were carried out at 25°C and repeated at least three times. The baselines of both spectra were subtracted. Only the mutants that varied from WT CK are displayed.