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• W2122387125 endingPage "1641" @default.
• W2122387125 startingPage "1630" @default.
• W2122387125 abstract "Abstract Spectral assignment of the IRMPD bands and identification of the vibrational signatures of deprotonated phosphorylated amino acids are attained. The H 2 PO 4 − anion is used as a simple model of a free deprotonated phosphate group to identify the IR signatures of phosphorylation. The fragmentation efficiency is lower for [pSer‐H] − (left scale in figure) than for [pThr‐H] − and [pTyr‐H] − (right scale). magnified image Gas‐phase infrared spectra of deprotonated phosphorylated amino acids ([pAA‐H] − )—phosphoserine ([pSer‐H] − ), phosphothreonine ([pThr‐H] − ), and phosphotyrosine ([pTyr‐H] − )—and of the dihydrogen phosphate anion H 2 PO 4 − have been recorded in the mid‐IR region (650–2000 cm −1 ) under tandem mass spectrometry conditions. The experimental setup involved a Paul ion trap equipped with an electrospray ionization source coupled with a tunable free electron laser (FEL). Spectral assignment of the observed IRMPD bands and identification of the vibrational signatures of the phosphorylation have been performed by comparison with DFT calculations. The H 2 PO 4 − anion has been used as a simple model of a free deprotonated phosphate group, helping the identification of the IR signatures of phosphorylation. Our results show that deprotonation occurs on the phosphate group for the three amino acids. A comparison between the deprotonated and protonated phosphorylated amino acids is reported for the most important vibrational features." @default.
• W2122387125 created "2016-06-24" @default.
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• W2122387125 date "2009-06-29" @default.
• W2122387125 modified "2023-10-11" @default.
• W2122387125 title "Structural Characterization by IRMPD Spectroscopy and DFT Calculations of Deprotonated Phosphorylated Amino Acids in the Gas Phase" @default.
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• W2122387125 doi "https://doi.org/10.1002/cphc.200800856" @default.
• W2122387125 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19347918" @default.
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