Article: Energy and entropy effects in dissociation of peptide radical anions
| Title | Energy and entropy effects in dissociation of peptide radical anions |
|---|---|
| Authors | Laskin, J3 Yang, Z1 3 Lam, C2 Chu, IK2 |
| Keywords | Activation Entropy Peptide Radical Anion Rrkm Modeling Side Chain Loss Surface-Induced Dissociation Threshold Energy |
| Issue Date | 2012 |
| Publisher | Elsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/ijms |
| Citation | International 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 |
| Abstract | Time- 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. |
| ISSN | 1387-3806 2011 Impact Factor: 2.549 2011 SCImago Journal Rankings: 0.182 |
| DOI | http://dx.doi.org/10.1016/j.ijms.2012.01.006 |
| References | References in Scopus |
| dc.contributor.author | Laskin, J |
|---|---|
| dc.contributor.author | Yang, Z |
| dc.contributor.author | Lam, C |
| dc.contributor.author | Chu, IK |
| dc.date.accessioned | 2012-10-08T03:23:48Z |
| dc.date.available | 2012-10-08T03:23:48Z |
| dc.date.issued | 2012 |
| dc.description.abstract | Time- 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.nature | Link_to_subscribed_fulltext |
| dc.identifier.citation | International 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.citeulike | 10267519 |
| dc.identifier.doi | http://dx.doi.org/10.1016/j.ijms.2012.01.006 |
| dc.identifier.epage | 258 |
| dc.identifier.hkuros | 208683 |
| dc.identifier.issn | 1387-3806 2011 Impact Factor: 2.549 2011 SCImago Journal Rankings: 0.182 |
| dc.identifier.scopus | eid_2-s2.0-84862789145 |
| dc.identifier.spage | 251 |
| dc.identifier.uri | http://hdl.handle.net/10722/168637 |
| dc.identifier.volume | 316-318 |
| dc.language | eng |
| dc.publisher | Elsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/ijms |
| dc.publisher.place | Netherlands |
| dc.relation.ispartof | International Journal of Mass Spectrometry |
| dc.relation.references | References in Scopus |
| dc.subject | Activation Entropy |
| dc.subject | Peptide Radical Anion |
| dc.subject | Rrkm Modeling |
| dc.subject | Side Chain Loss |
| dc.subject | Surface-Induced Dissociation |
| dc.subject | Threshold Energy |
| dc.title | Energy and entropy effects in dissociation of peptide radical anions |
| dc.type | Article |
Author Affiliations
- University of Colorado at Boulder
- The University of Hong Kong
- Pacific Northwest National Laboratory