Polarized Raman spectra and intensities of aromatic amino acids phenylalanine, tyrosine and tryptophan

Wolfgang B. Fischer, Hans H. Eysel*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

The prominent marker bands in the Raman spectra of the aromatic proteinogenic amino acids phenylalanine, tryptophan and tyrosine have been reinvestigated. Previous studies have been extended by measuring intensities against NaClO4 as an external standard. Raman spectra were divided into isotropic (trace scattering of symmetric vibrations) and anisotropic (quadrupole scattering of antisymmetric or symmetric vibrations). These intensity and polarization properties of the marker bands were followed through pH changes from about 11-13 to 1-2.

Original languageEnglish
Pages (from-to)725-732
Number of pages8
JournalSpectrochimica Acta Part A: Molecular Spectroscopy
Volume48
Issue number5
DOIs
StatePublished - May 1992

Fingerprint

Dive into the research topics of 'Polarized Raman spectra and intensities of aromatic amino acids phenylalanine, tyrosine and tryptophan'. Together they form a unique fingerprint.

Cite this