title: Chromophore conformational analysis in phycocyanin and in related chromopeptides by surface enhanced Raman spectroscopy.
abstract: 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.
authors.affiliation: Institute of Biophysics, Hungarian Academy of Sciences, Szeged.
authors.forename: M
authors.initials: M
authors.lastname: Debreczeny
authors.forename: Z
authors.initials: Z
authors.lastname: Gombos
authors.forename: V
authors.initials: V
authors.lastname: Csizmadia
authors.forename: Z
authors.initials: Z
authors.lastname: Várkonyi
authors.forename: B
authors.initials: B
authors.lastname: Szalontai
mesh_terms: D010446:Peptide Fragments; D010798:Phycocyanin / Q000302:isolation & purification; D010860:Pigments, Biological / Q000302:isolation & purification; D011487:Protein Conformation; D013053:Spectrophotometry; D013059:Spectrum Analysis, Raman / Q000379:methods
chemical_list: D010446:Peptide Fragments; D010860:Pigments, Biological; D010798:Phycocyanin