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Article: Effect of the basic residue on the energetics, dynamics, and mechanisms of gas-phase fragmentation of protonated peptides
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TitleEffect of the basic residue on the energetics, dynamics, and mechanisms of gas-phase fragmentation of protonated peptides
 
AuthorsLaskin, J2
Yang, Z2
Song, T1
Lam, C1
Chu, IK1
 
Issue Date2010
 
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
 
CitationJournal Of The American Chemical Society, 2010, v. 132 n. 45, p. 16006-16016 [How to Cite?]
DOI: http://dx.doi.org/10.1021/ja104438z
 
AbstractThe effect of the basic residue on the energetics, dynamics, and mechanisms of backbone fragmentation of protonated peptides was investigated. Time-resolved and collision energy-resolved surface-induced dissociation (SID) of singly protonated peptides with the N-terminal arginine residue and their analogues, in which arginine is replaced with less basic lysine and histidine residues, was examined using a specially configured Fourier transform ion cyclotron resonance mass spectrometer (FTICR-MS). SID experiments demonstrated different kinetics of formation of several primary product ions of peptides with and without arginine residue. The energetics and dynamics of these pathways were determined from Rice-Ramsperger-Kassel-Marcus (RRKM) modeling of the experimental data. Comparison between the kinetics and energetics of fragmentation of arginine-containing peptides and the corresponding methyl ester derivatives provides important information on the effect of dissociation pathways involving salt bridge (SB) intermediates on the observed fragmentation behavior. Because pathways involving SB intermediates are characterized by low threshold energies, they efficiently compete with classical oxazolone and imine/enol pathways of arginine-containing peptides on a long time scale of the FTICR instrument. In contrast, fragmentation of histidine- and lysine-containing peptides is largely determined by canonical pathways. Because SB pathways are characterized by negative activation entropies, fragmentation of arginine-containing peptides is kinetically hindered and observed at higher collision energies as compared to their lysine- and histidine-containing analogues. © 2010 American Chemical Society.
 
ISSN0002-7863
2012 Impact Factor: 10.677
2012 SCImago Journal Rankings: 5.182
 
DOIhttp://dx.doi.org/10.1021/ja104438z
 
ISI Accession Number IDWOS:000284202200043
Funding AgencyGrant Number
Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the U.S. Department of Energy (DOE)
University of Hong Kong and Hong Kong Research Grant Council, Special Administrative Region, China7012/08P
DOE's Office of Biological and Environmental Research
DOEDE-AC05-76RL01830
Funding Information:

This study was partially supported by the grant from the Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the U.S. Department of Energy (DOE), and the University of Hong Kong and Hong Kong Research Grant Council, Special Administrative Region, China (Project No. 7012/08P). The research described in this article was performed at the DOE's W.R. Wiley Environmental Molecular Sciences Laboratory (EMSL), a national scientific user facility sponsored by the DOE's Office of Biological and Environmental Research and located at Pacific Northwest National Laboratory (PNNL). PNNL is operated by Battelle for the DOE under Contract DE-AC05-76RL01830.

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorLaskin, J
 
dc.contributor.authorYang, Z
 
dc.contributor.authorSong, T
 
dc.contributor.authorLam, C
 
dc.contributor.authorChu, IK
 
dc.date.accessioned2011-07-27T01:26:14Z
 
dc.date.available2011-07-27T01:26:14Z
 
dc.date.issued2010
 
dc.description.abstractThe effect of the basic residue on the energetics, dynamics, and mechanisms of backbone fragmentation of protonated peptides was investigated. Time-resolved and collision energy-resolved surface-induced dissociation (SID) of singly protonated peptides with the N-terminal arginine residue and their analogues, in which arginine is replaced with less basic lysine and histidine residues, was examined using a specially configured Fourier transform ion cyclotron resonance mass spectrometer (FTICR-MS). SID experiments demonstrated different kinetics of formation of several primary product ions of peptides with and without arginine residue. The energetics and dynamics of these pathways were determined from Rice-Ramsperger-Kassel-Marcus (RRKM) modeling of the experimental data. Comparison between the kinetics and energetics of fragmentation of arginine-containing peptides and the corresponding methyl ester derivatives provides important information on the effect of dissociation pathways involving salt bridge (SB) intermediates on the observed fragmentation behavior. Because pathways involving SB intermediates are characterized by low threshold energies, they efficiently compete with classical oxazolone and imine/enol pathways of arginine-containing peptides on a long time scale of the FTICR instrument. In contrast, fragmentation of histidine- and lysine-containing peptides is largely determined by canonical pathways. Because SB pathways are characterized by negative activation entropies, fragmentation of arginine-containing peptides is kinetically hindered and observed at higher collision energies as compared to their lysine- and histidine-containing analogues. © 2010 American Chemical Society.
 
dc.description.natureLink_to_subscribed_fulltext
 
dc.identifier.citationJournal Of The American Chemical Society, 2010, v. 132 n. 45, p. 16006-16016 [How to Cite?]
DOI: http://dx.doi.org/10.1021/ja104438z
 
dc.identifier.doihttp://dx.doi.org/10.1021/ja104438z
 
dc.identifier.epage16016
 
dc.identifier.hkuros186187
 
dc.identifier.isiWOS:000284202200043
Funding AgencyGrant Number
Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the U.S. Department of Energy (DOE)
University of Hong Kong and Hong Kong Research Grant Council, Special Administrative Region, China7012/08P
DOE's Office of Biological and Environmental Research
DOEDE-AC05-76RL01830
Funding Information:

This study was partially supported by the grant from the Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the U.S. Department of Energy (DOE), and the University of Hong Kong and Hong Kong Research Grant Council, Special Administrative Region, China (Project No. 7012/08P). The research described in this article was performed at the DOE's W.R. Wiley Environmental Molecular Sciences Laboratory (EMSL), a national scientific user facility sponsored by the DOE's Office of Biological and Environmental Research and located at Pacific Northwest National Laboratory (PNNL). PNNL is operated by Battelle for the DOE under Contract DE-AC05-76RL01830.

 
dc.identifier.issn0002-7863
2012 Impact Factor: 10.677
2012 SCImago Journal Rankings: 5.182
 
dc.identifier.issue45
 
dc.identifier.openurl
 
dc.identifier.pmid20977217
 
dc.identifier.scopuseid_2-s2.0-78449244153
 
dc.identifier.spage16006
 
dc.identifier.urihttp://hdl.handle.net/10722/135026
 
dc.identifier.volume132
 
dc.languageeng
 
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
 
dc.publisher.placeUnited States
 
dc.relation.ispartofJournal of the American Chemical Society
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshArginine - chemistry
 
dc.subject.meshEntropy
 
dc.subject.meshGases - chemistry
 
dc.subject.meshOligopeptides - chemistry
 
dc.subject.meshPeptide Fragments - chemistry
 
dc.titleEffect of the basic residue on the energetics, dynamics, and mechanisms of gas-phase fragmentation of protonated peptides
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong
  2. Pacific Northwest National Laboratory