Raman and Fourier transform infrared study of yeast alcohol dehydrogenase

Raman spectra of yeast alcohol dehydrogenase in buffered, aqueous solutions and in D₂O, and FTIR spectra of aqueous solutions and thin films have been collected and analyzed. No significant differences between the Raman spectra in the pH range 6.00–7.50 and between the infrared spectra of the solution and film have been observed. The tyrosine doublet strongly favors exposed hydroxyl groups and the Raman spectra indicate multiple conformations for the disulfide moieties. Analysis of Raman intensities favors significant α‐helix and random coil contents. The secondary structure of yeast alcohol dehydrogenase based on Raman data is compared with the better characterized secondary structure of equine liver alcohol dehydrogenase.