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Article: Energy and entropy effects in dissociation of peptide radical anions
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TitleEnergy and entropy effects in dissociation of peptide radical anions
 
AuthorsLaskin, J3
Yang, Z2 3
Lam, C1
Chu, IK1
 
KeywordsActivation Entropy
Peptide Radical Anion
Rrkm Modeling
Side Chain Loss
Surface-Induced Dissociation
Threshold Energy
 
Issue Date2012
 
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/ijms
 
CitationInternational Journal Of Mass Spectrometry, 2012, v. 316-318, p. 251-258 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.ijms.2012.01.006
 
AbstractTime- and collision energy-resolved surface-induced dissociation (SID) of peptide radical anions was studied using a Fourier transform ion cyclotron resonance mass spectrometer (FT-ICR MS) configured for SID experiments. Peptide radical cations and anions were produced by gas-phase fragmentation of Co III(salen)-peptide complexes. The effect of the charge, radical, and the presence of a basic residue on the energetics and dynamics of dissociation of peptide ions was examined using RVYIHPF (1) and HVYIHPF (2) as model systems. Comparison of the survival curves of [M+H] +, [M-H] -, M +, and [M-2H] - ions of these precursors demonstrated that even-electron ions are more stable toward fragmentation than their odd-electron counterparts. RRKM modeling of the experimental data demonstrated that the lower stability of the positive radicals is mainly attributed to lower dissociation thresholds while entropy effects are responsible the relative instability of the negative radicals. Substitution of arginine with less basic histidine residue has a strong destabilizing effect on the [M+H] + ions and a measurable stabilizing effect on the odd-electron ions. Lower threshold energies for dissociation of both positive and negative radicals of 1 are attributed to the presence of lower-energy dissociation pathways that are most likely promoted by the presence of arginine. © 2011 Elsevier B.V. All rights reserved.
 
ISSN1387-3806
2013 Impact Factor: 2.227
2013 SCImago Journal Rankings: 0.886
 
DOIhttp://dx.doi.org/10.1016/j.ijms.2012.01.006
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorLaskin, J
 
dc.contributor.authorYang, Z
 
dc.contributor.authorLam, C
 
dc.contributor.authorChu, IK
 
dc.date.accessioned2012-10-08T03:23:48Z
 
dc.date.available2012-10-08T03:23:48Z
 
dc.date.issued2012
 
dc.description.abstractTime- and collision energy-resolved surface-induced dissociation (SID) of peptide radical anions was studied using a Fourier transform ion cyclotron resonance mass spectrometer (FT-ICR MS) configured for SID experiments. Peptide radical cations and anions were produced by gas-phase fragmentation of Co III(salen)-peptide complexes. The effect of the charge, radical, and the presence of a basic residue on the energetics and dynamics of dissociation of peptide ions was examined using RVYIHPF (1) and HVYIHPF (2) as model systems. Comparison of the survival curves of [M+H] +, [M-H] -, M +, and [M-2H] - ions of these precursors demonstrated that even-electron ions are more stable toward fragmentation than their odd-electron counterparts. RRKM modeling of the experimental data demonstrated that the lower stability of the positive radicals is mainly attributed to lower dissociation thresholds while entropy effects are responsible the relative instability of the negative radicals. Substitution of arginine with less basic histidine residue has a strong destabilizing effect on the [M+H] + ions and a measurable stabilizing effect on the odd-electron ions. Lower threshold energies for dissociation of both positive and negative radicals of 1 are attributed to the presence of lower-energy dissociation pathways that are most likely promoted by the presence of arginine. © 2011 Elsevier B.V. All rights reserved.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationInternational Journal Of Mass Spectrometry, 2012, v. 316-318, p. 251-258 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.ijms.2012.01.006
 
dc.identifier.citeulike10267519
 
dc.identifier.doihttp://dx.doi.org/10.1016/j.ijms.2012.01.006
 
dc.identifier.epage258
 
dc.identifier.hkuros208683
 
dc.identifier.issn1387-3806
2013 Impact Factor: 2.227
2013 SCImago Journal Rankings: 0.886
 
dc.identifier.scopuseid_2-s2.0-84862789145
 
dc.identifier.spage251
 
dc.identifier.urihttp://hdl.handle.net/10722/168637
 
dc.identifier.volume316-318
 
dc.languageeng
 
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/ijms
 
dc.publisher.placeNetherlands
 
dc.relation.ispartofInternational Journal of Mass Spectrometry
 
dc.relation.referencesReferences in Scopus
 
dc.subjectActivation Entropy
 
dc.subjectPeptide Radical Anion
 
dc.subjectRrkm Modeling
 
dc.subjectSide Chain Loss
 
dc.subjectSurface-Induced Dissociation
 
dc.subjectThreshold Energy
 
dc.titleEnergy and entropy effects in dissociation of peptide radical anions
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong
  2. University of Colorado at Boulder
  3. Pacific Northwest National Laboratory