Article (Scientific journals)
Discrimination of Isobaric Leu/Ile Residues by MALDI In-source Decay Mass Spectrometry
Asakawa, Daiki; Smargiasso, Nicolas; De Pauw, Edwin
2013In Journal of the American Society for Mass Spectrometry, 24 (2), p. 297-300
Peer Reviewed verified by ORBi
 

Files


Full Text
2012-5390-2.pdf
Author preprint (2.8 MB)
Request a copy

All documents in ORBi are protected by a user license.

Send to



Details



Keywords :
Top down sequencing; MALDI ISD; LEU/ILEU
Abstract :
[en] MALDI in-source decay (ISD) has been used for the top-down sequencing of proteins. The use of 1,5-diaminonapthalene (1,5-DAN) gave strong intensity of w ions, which are informative fragments and can be helpful for the distinction of the isobaric amino acids, Leu and Ile. Our data suggests that the w fragments are formed from z* radical fragment by unimolecular dissociation and high abundance of w ions in MALDI-ISD with 1,5-DAN can be understood as resulting from the low collision rate in the MALDI plume. The MALDI-ISD with 1,5-DAN could be a useful method for the top-down sequencing of proteins including discrimination of Leu and Ile near the C-terminal end.
Research center :
Giga-Systems Biology and Chemical Biology - ULiège
Disciplines :
Chemistry
Biochemistry, biophysics & molecular biology
Author, co-author :
Asakawa, Daiki
Smargiasso, Nicolas ;  Université de Liège - ULiège > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.)
De Pauw, Edwin  ;  Université de Liège - ULiège > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.)
Language :
English
Title :
Discrimination of Isobaric Leu/Ile Residues by MALDI In-source Decay Mass Spectrometry
Publication date :
February 2013
Journal title :
Journal of the American Society for Mass Spectrometry
ISSN :
1044-0305
eISSN :
1879-1123
Publisher :
Spinger, New York, United States
Volume :
24
Issue :
2
Pages :
297-300
Peer reviewed :
Peer Reviewed verified by ORBi
European Projects :
FP7 - 278346 - VENOMICS - High-throughput peptidomics and transcriptomics of animal venoms for discovery of novel therapeutic peptides and innovative drug development
Funders :
F.R.S.-FNRS - Fonds de la Recherche Scientifique [BE]
JSPS - Japan Society for the Promotion of Science [JA]
CE - Commission Européenne [BE]
Available on ORBi :
since 25 September 2012

Statistics


Number of views
126 (13 by ULiège)
Number of downloads
4 (1 by ULiège)

Scopus citations®
 
30
Scopus citations®
without self-citations
12
OpenCitations
 
30

Bibliography


Similar publications



Contact ORBi