Chromophore conformational analysis in phycocyanin and in related chromopeptides by surface enhanced Raman spectroscopy

M. Debreczeny, Z. Gombos, V. Csizmadia, Zs Várkonyl, B. Szalontai

Research output: Contribution to journalArticle

5 Citations (Scopus)


Chromopeptides got from phycocyanin by proteolytic digestion do not preserve the extended chromophore conformations characteristic to the native protein. Chromophore conformations in the chromopeptides showed heterogenity varying between completely folded and semi-extended states. Indications were found that the silver sol-phycocyanin interaction involves the UV electronic transition of the biliprotein which may explain why the visible excited surface enhanced Raman spectra were similar not to the visible excited but to the UV-excited resonance Raman spectrum of phycocyanin.

Original languageEnglish
Pages (from-to)1227-1232
Number of pages6
JournalBiochemical and biophysical research communications
Issue number3
Publication statusPublished - Mar 31 1989


ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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