Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1997-2-14
pubmed:abstractText
Effective analysis of the sequence of peptides using matrix-assisted laser desorption/ionization (MALDI) tandem ion trap mass spectrometry requires efficient mass isolation and the ability to induce extensive sequence-specific fragmentation. The present paper describes a new excitation scheme, which we term red-shifted off-resonance large-amplitude excitation (RSORLAE), that can deposit higher amounts of internal energy in ions than is feasible with conventional resonant excitation. The new method provides an effective means for inducing fragmentation of MALDI-produced peptide ions with m/z values up to 3500. Prior to excitation, it is necessary to isolate ions of interest with high efficiency. We demonstrate that isolation efficiencies of > 95% can be achieved by careful design of the rf scan functions used during ion isolation. In particular, sudden transitions in the amplitude of the rf field (from low to high amplitudes) must be avoided. The combined improvements in the efficiency for ion isolation and the efficacy of ion activation make MALDI tandem ion trap mass spectrometry a practical tool for the characterization of proteins with high sensitivity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0003-2700
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
68
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2108-12
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Matrix-assisted laser desorption ion trap mass spectrometry: efficient isolation and effective fragmentation of peptide ions.
pubmed:affiliation
Rockefeller University, New York, New York 10021, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.