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Raman and Fourier transform infrared study of yeast alcohol dehydrogenase
Author(s) -
Hall William H.,
Jagodzinski Paul W.
Publication year - 1987
Publication title -
journal of raman spectroscopy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.748
H-Index - 110
eISSN - 1097-4555
pISSN - 0377-0486
DOI - 10.1002/jrs.1250180210
Subject(s) - raman spectroscopy , chemistry , aqueous solution , alcohol dehydrogenase , fourier transform infrared spectroscopy , random coil , analytical chemistry (journal) , infrared , alcohol , protein secondary structure , biochemistry , chromatography , optics , physics
Raman spectra of yeast alcohol dehydrogenase in buffered, aqueous solutions and in D 2 O, 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.