Journalartikel
Autorenliste: Spengler, B; Hester, A
Jahr der Veröffentlichung: 2008
Seiten: 1808-1812
Zeitschrift: Journal of The American Society for Mass Spectrometry
Bandnummer: 19
Heftnummer: 12
ISSN: 1044-0305
DOI Link: https://doi.org/10.1016/j.jasms.2008.08.005
Verlag: American Chemical Society
Abstract:
Accurate mass values as obtainable by Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) were employed in a theoretical study to differentiate between nonmodified and phosphorylated peptides. It was found that for peptide masses up to 1000 u more than 98% of all theoretical monophosphorylated. peptides (all possible combinations of proteinogenic amino acids having one phosphorylation on S, T, or Y) can be distinguished from nonphosphorylated peptides directly by their mass, if mass values are determined with an accuracy of better than +/- 0.1 ppm. At a peptide mass of 1500 u still 70% of all possible monophosphorylated peptides are distinguishable from nonmodified peptides by their accurate mass alone. In contrast to established techniques of data-dependent multidimensional mass spectrometry, only the mass of the precursor ion is necessary to decide upon subsequent fragment ion analysis of a peptide for sequence analysis in an LC-MS/MS investigation of a complex sample, when using a precalculated mass distribution table of theoretical peptides. A mass distribution table of nonphosphorylated and monophosphorylated peptides with a bin width of 0.1 mu was made available via the open web site www.peptidecomposer.com.
Zitierstile
Harvard-Zitierstil: Spengler, B. and Hester, A. (2008) Mass-Based Classification (MBC) of Peptides: Highly Accurate Precursor Ion Mass Values Can Be Used to Directly Recognize Peptide Phosphorylation, Journal of The American Society for Mass Spectrometry, 19(12), pp. 1808-1812. https://doi.org/10.1016/j.jasms.2008.08.005
APA-Zitierstil: Spengler, B., & Hester, A. (2008). Mass-Based Classification (MBC) of Peptides: Highly Accurate Precursor Ion Mass Values Can Be Used to Directly Recognize Peptide Phosphorylation. Journal of The American Society for Mass Spectrometry. 19(12), 1808-1812. https://doi.org/10.1016/j.jasms.2008.08.005