Journalartikel

Jahr der Veröffentlichung: 1993

Seiten: 1482-1490

Zeitschrift: Organic Mass Spectrometry

Bandnummer: 28

Heftnummer: 12

ISSN: 0030-493X

DOI Link: https://doi.org/10.1002/oms.1210281220

Verlag: Wiley

Abstract: 
Hydrogen-deuterium exchange was evaluated as a tool for sequence analysis of peptides by matrix-assisted laser desorption-ionization utilizing post-source decay (PSD-MALDI). The number of exchangeable hydrogens (EH) of precursor ions and product ions can be determined from the mass difference between ion signals originating from the deuterated and the non-deuterated form of a peptide, resulting in a second dimension of structural information. The reliability of sequence determination by combinatorial algorithms or pattern recognition techniques is considerably increased by employing this 'EH spectroscopy.' On-target deuteration is a simple preparatory step which can be performed reversibly with the already mass-analysed sample within a few minutes and without consumption of additional sample material. The efficiency of hydrogen-deuterium exchange with this technique is about 98.5%. In addition to supporting sequence analysis, deuteration can be used to investigate fundamental fragmentation mechanisms of peptides in PSD-MALDI. Inconsistencies with expected fragmentation pathways have been found for fragments a1-a3 of substance P.

Harvard-Zitierstil: Spengler, B., Lützenkrichen, F. and Kaufmann, R. (1993) On‐target deuteration for peptide sequencing by laser mass spectrometry, Organic Mass Spectrometry, 28(12), pp. 1482-1490. https://doi.org/10.1002/oms.1210281220

APA-Zitierstil: Spengler, B., Lützenkrichen, F., & Kaufmann, R. (1993). On‐target deuteration for peptide sequencing by laser mass spectrometry. Organic Mass Spectrometry. 28(12), 1482-1490. https://doi.org/10.1002/oms.1210281220