By a News Reporter-Staff News Editor at Life Science Weekly -- Data detailed on Amino Acids have been presented. According to news reporting out of Sart Tilman Par Liege, Belgium, by NewsRx editors, research stated, "The type of ions detected after in-source decay (ISD) in a MALDI source differs according to the ion source pressure and on the mass analyzer used. We present the mechanism leading to the final ISD ions for a Fourier transform-ion cyclotron resonance mass spectrometer (FTICR MS)."
Our news journalists obtained a quote from the research from the University of Liege, "The MALDI ion source was operated at intermediate pressure to cool the resulting ions and increase their lifetime during the long residence times in the FTICR ion optics. This condition produces not only c', z', and w fragments, but also a, y', and d fragments. In particular, d ions help to identify isobaric amino acid residues present near the N-terminal amino acid. Desorbed ions collide with background gas during desorption, leading to proton mobilization from Arg residues to a less favored protonation site. As a result, in the case of ISD with MALDI FTICR, the influence of the Arg residue in ISD fragmentation is less straightforward than for TOF MS and the sequence coverage is thus improved. MALDI-ISD combined with FTICR MS appears to be a useful method for sequencing of peptides and proteins including discrimination of isobaric amino acid residues and site determination of phosphorylation. Additionally we also used new software for in silico elimination of MALDI matrix peaks from MALDI-ISD FTICR mass spectra. The combination of high resolving power of an FTICR analyzer and matrix subtraction software helps to interpret the low m/z region of MALDI-ISD spectra."
According to the news editors, the research concluded: "Finally, several of these developed methods are applied in unison toward a MALDI ISD FTICR imaging experiment on mouse brain to achieve better results."
For more information on this research see: In-Source Decay during Matrix-Assisted Laser Desorption/Ionization Combined with the Collisional Process in an FTICR Mass Spectrometer. Analytical Chemistry, 2013;85(16):7809-7817. Analytical Chemistry can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Analytical Chemistry - www.pubs.acs.org/journal/ancham)
Our news journalists report that additional information may be obtained by contacting D. Asakawa, University of Liege, GIGA Res, B-4000 Sart Tilman Par Liege, Belgium. Additional authors for this research include D. Calligaris, T.A. Zimmerman and E. De Pauw (see also Amino Acids).
Keywords for this news article include: Europe, Belgium, Peptides, Proteins, Software, Amino Acids, Sart Tilman Par Liege
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