Peptide sequencing of charged derivatives by postsource decay MALDI mass spectrometry

Spengler, B., Luetzenkirchen, F., Metzger, S., Chaurand, P., Kaufmann, R., Jeffery, W., Bartlet-Jones, M., Pappin, D. J. C. (1997) Peptide sequencing of charged derivatives by postsource decay MALDI mass spectrometry. International Journal of Mass Spectrometry and Ion Processes, 169-17. pp. 127-140. ISSN 01681176 (ISSN)

DOI: 10.1016/S0168-1176(97)00218-8


Derivatization procedures for peptides are described that can be performed with sub-picomolar amounts of sample and that are able to direct the formation of fragment ions in Postsource Decay (PSD) MALDI mass spectrometry. Location of a fixed charge (a quarternary ammonium ion) at the N-terminus of a peptide and modification of internal arginine residues (deletion of strong basicity) leads to a full controllability of fragment ion formation resulting in mostly complete series of N-terminal fragment ions. The method appears to be favorably applicable to sequence analysis of unknown peptides, since in most cases the amino acid sequence can directly be read from the spectrum. © 1997 Elsevier Science B.V.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > design > amino acid design
bioinformatics > genomics and proteomics > design > protein network design > peptide design
Investigative techniques and equipment > spectroscopy > mass spectrometry
CSHL Authors:
Communities: CSHL labs > Pappin lab
Depositing User: Kathleen Darby
Date: 1997
Date Deposited: 07 May 2014 14:36
Last Modified: 24 Feb 2017 17:08

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving