[Analytical description of electron-vibrational protein spectra].
Electron-vibrational spectra of phosphorescence and fluorescence of tryptophan residues in proteins at 77 K are best approximated by theoretical curves computed according to a model which suggests the existence of two independent series of Gaussian vibrational components. Each series contains one type of vibrations. Phosphorescence and fluorescence spectra of proteins with various localizations of their single tryptophan residue were fitted by a curve computed according to this model. The results obtained show that the phosphorescence band of tryptophan residues in proteins seems to contain two types of vibrations with frequencies 650-800 cm-1 and 1350-1500 cm-1. Since the substitution of H2O by D2O does not change the frequencies of both vibrations in the phosphorescence spectra of human serum albumin, melittin and tryptophan in 1 M KCl, it is reasonable to suggest that the 1350-1500 cm-1 series corresponds to the W5 type vibrations (B19a type of vibrations of benzene ring). The 650-800 cm-1 series"can be identified with W18 type of vibrations (breathing vibrations of indole ring). Phosphorescence parameters of tryptophan residues in proteins correlate with their fluorescence parameters.
Permiakov
E A
EA
Deĭkus
G Iu
GIu
D000818:Animals; D004583:Electrons; D005399:Fishes; D005453:Fluorescence; D006801:Humans; D008555:Melitten / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012709:Serum Albumin / Q000737:chemistry; D013057:Spectrum Analysis; D014364:Tryptophan / Q000737:chemistry
D011506:Proteins; D012709:Serum Albumin; D008555:Melitten; D014364:Tryptophan
Analiticheskoe opisanie élektronno-kolebatel'nykh spelktrov belkov.