Raman spectra of porcine mitochondrial malate dehydrogenase have been collected and analysed. The existence of weak hydrogen bonds is indicated by the intensity ratio of the tyrosine doublet and a band is found which can be attributed to disulfide bonds. The observed frequencies in the amide I and III regions favor significant contributions from α‐helix and random conformations. An analysis of the intensities using standard methods predicts a very low β‐sheet content.
ASJC Scopus subject areas
- Materials Science(all)