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Vibrational signatures of protonated, phosphorylated amino acids in the gas phase

Domenii publicaţii > Chimie + Tipuri publicaţii > Articol în revistã ştiinţificã

Autori: Catarina F. Correia, Petru O. Balaj, Debora Scuderi, Philippe Maitre, and Gilles Ohanessian

Editorial: J. Am. Chem. Soc., 130 (11), p.3359–3370, 2008.


Structural characterization of protonated phosphorylated serine, threonine, and tyrosine was performed using mid-infrared multiple photon dissociation (IRMPD) spectroscopy and density functional theory (DFT) calculations. The ions were generated and analyzed by an external electrospray source coupled to a Paul ion-trap type mass spectrometer. Their fragmentation was induced by the resonant absorption of multiple photons from a tunable free electron laser (FEL) beam. IRMPD spectra were recorded in the 900-1850 cm-1 energy range and compared to the corresponding computed IR spectra. On the basis of the frequency and intensity of two independent bands in the 900-1400 cm-1 energy range, it is possible to identify the phosphorylated residue. IRMPD spectra for a 12-residue fragment of stathmin in its phosphorylated and nonphosphorylated forms were also recorded in the 800-1400 cm-1 energy range.
The lack of spectral congestion in the 900-1300 cm-1 region makes their distinction facile. Our results show that IRMPD spectroscopy may became a valuable tool for structural characterization of small phosphorylated peptides.

Cuvinte cheie: protonated phosphorylated serine, threonine, and tyrosine, gas phase, IRMPD spectroscopy,