Linked Life Data

15103103

Source:http://linkedlifedata.com/resource/pubmed/id/15103103

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-4-22
pubmed:abstractText
This account summarizes the energetics and dynamics of peptide fragmentation obtained using a new approach recently developed in our laboratory. The approach involves RRKM modeling of time- and energy- resolved tandem mass spectrometry (MS/MS) data obtained using collisional activation. We demonstrate that surface-induced dissociation (SID) on a long time-scale of Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) is perfectly suited for studying the energetics and dynamics of peptide fragmentation. The advantages provided by SID include very fast ion activation, which eliminates possible discrimination against higher-energy dissociation pathways, and efficient "amplification" of small changes in dissociation parameters. We present a summary of results obtained for small alanine-containing peptides as well as larger peptides including angiotensin analogs and a series of peptides containing the LDIFSDF motif.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1469-0667
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
259-67
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Energetics and dynamics of peptide fragmentation from multiple-collision activation and surface-induced dissociation studies.
pubmed:affiliation
Fundamental Science Directorate, Pacific Northwest National Laboratory, PO Box 999 (K8-88), Richland, WA 99352, USA. Julia.Laskin@pnl.gov
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.