Raman and Fourier transform infrared study of yeast alcohol dehydrogenase

William H. Hall, Paul W. Jagodzinski

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)119-122
Number of pages4
JournalJournal of Raman Spectroscopy
Volume18
Issue number2
DOIs
StatePublished - Mar 1987
Externally publishedYes

ASJC Scopus subject areas

  • Materials Science(all)
  • Spectroscopy

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