Please use this identifier to cite or link to this item:
http://hdl.handle.net/1942/20686
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lermyte, Frederik | - |
dc.contributor.author | Lacki, Mateusz Krzysztof | - |
dc.contributor.author | VALKENBORG, Dirk | - |
dc.contributor.author | Baggerman, Geert | - |
dc.contributor.author | Gambin, Anna | - |
dc.contributor.author | Sobott, Frank | - |
dc.date.accessioned | 2016-02-18T09:12:10Z | - |
dc.date.available | 2016-02-18T09:12:10Z | - |
dc.date.issued | 2015 | - |
dc.identifier.citation | INTERNATIONAL JOURNAL OF MASS SPECTROMETRY, 390, p. 146-154 | - |
dc.identifier.issn | 1387-3806 | - |
dc.identifier.uri | http://hdl.handle.net/1942/20686 | - |
dc.description.abstract | Electron transfer dissociation (ETD) is becoming increasingly more important in mass spectrometrybased structural proteomics due to its ability to cleave the protein backbone without annihilating the higher-order structure. Concomitant with ETD, non-dissociative charge reduction occurs primarily by proton transfer from the protein precursor to the ETD reagent, and by non-dissociative electron transfer from the reagent to the protein. While it has been known for some time that the preference for either proton or electron transfer is largely a function of the properties of the reagent, the extent of dissociative versus non-dissociative electron transfer is also dependent on instrument choice, precursor charge state and conformation, as well as ion activation before, during, and after cation/anion interaction. In this work, we use a novel software named MASSTODON to quantify the different reaction pathways in top-down spectra of ubiquitin, acquired on two different instruments: a Synapt G2 (Waters) and an LTQ Orbitrap Velos (Thermo). We compare the behavior of different precursor charge states, representing more folded or more extended conformations, and also evaluate the effect of increasing supplemental activation (on the Synapt) and reaction time (on the Orbitrap). In agreement with previous work, increasing supplemental activation promotes fragment release and hydrogen radical migration from (N-terminal) c fragments to (C-terminal) z fragments. A longer reaction time leads to increasingly more extensive charge reduction and a decrease in the relative occurrence of non-dissociative electron transfer compared to proton transfer, possibly indicating some degree of time- andtharge-state dependent loss of electrostatic interactions on a timescale of a few tens of milliseconds. (C) 2015 Elsevier B.V. All rights reserved. | - |
dc.description.sponsorship | We thank the Research Foundation - Flanders (FWO) for funding a PhD fellowship (F.L.). The Synapt G2 mass spectrometer is funded by a grant from the Hercules Foundation - Flanders. Financial support from the Flemish Institute for Technological Research (VITO) is gratefully acknowledged. The authors also thank the FWO and the Polish Academy of Sciences for facilitating this collaboration via the project "Innovative algorithms to Detect Protein Modifications in Mass Spectrometry Data" (project number VS.005.13N). The authors also thank the reviewers for their valuable comments. | - |
dc.language.iso | en | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.rights | © 2015 Elsevier B.V. All rights reserved. | - |
dc.subject.other | Top-down mass spectrometry; Intact protein mass spectrometry; Top-down sequencing; Electron transfer dissociation; Data processing; Bioinformatics | - |
dc.subject.other | top-down mass spectrometry; intact protein mass spectrometry; top-down sequencing; electron transfer dissociation; data processing; bioinformatics | - |
dc.title | Understanding reaction pathways in top-down ETD by dissecting isotope distributions: A mammoth task | - |
dc.type | Journal Contribution | - |
dc.identifier.epage | 154 | - |
dc.identifier.spage | 146 | - |
dc.identifier.volume | 390 | - |
local.format.pages | 9 | - |
local.bibliographicCitation.jcat | A1 | - |
dc.description.notes | [Lermyte, Frederik; Sobott, Frank] Univ Antwerp, Dept Chem, Biomol & Analyt Mass Spectrometry Grp, B-2020 Antwerp, Belgium. [Lermyte, Frederik; Valkenborg, Dirk; Baggerman, Geert; Sobott, Frank] Univ Antwerp, UA VITO Ctr Prote, B-2020 Antwerp, Belgium. [Lacki, Mateusz Krzysztof; Gambin, Anna] Univ Warsaw, Inst Informat, PL-00325 Warsaw, Poland. [Valkenborg, Dirk] Hasselt Univ, Interuniv Inst Biostat & Stat Bioinformat, Hasselt, Belgium. [Valkenborg, Dirk; Baggerman, Geert] Flemish Inst Technol Res VITO, Appl Bio & Mol Syst, Antwerp, Belgium. | - |
local.publisher.place | AMSTERDAM | - |
local.type.refereed | Refereed | - |
local.type.specified | Article | - |
dc.identifier.doi | 10.1016/j.ijms.2015.08.008 | - |
dc.identifier.isi | 000366079600019 | - |
item.fulltext | With Fulltext | - |
item.fullcitation | Lermyte, Frederik; Lacki, Mateusz Krzysztof; VALKENBORG, Dirk; Baggerman, Geert; Gambin, Anna & Sobott, Frank (2015) Understanding reaction pathways in top-down ETD by dissecting isotope distributions: A mammoth task. In: INTERNATIONAL JOURNAL OF MASS SPECTROMETRY, 390, p. 146-154. | - |
item.accessRights | Restricted Access | - |
item.validation | ecoom 2017 | - |
item.contributor | Lermyte, Frederik | - |
item.contributor | Lacki, Mateusz Krzysztof | - |
item.contributor | VALKENBORG, Dirk | - |
item.contributor | Baggerman, Geert | - |
item.contributor | Gambin, Anna | - |
item.contributor | Sobott, Frank | - |
crisitem.journal.issn | 1387-3806 | - |
crisitem.journal.eissn | 1873-2798 | - |
Appears in Collections: | Research publications |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
lemyte 1.pdf Restricted Access | Published version | 2.2 MB | Adobe PDF | View/Open Request a copy |
SCOPUSTM
Citations
12
checked on Sep 2, 2020
WEB OF SCIENCETM
Citations
17
checked on May 8, 2024
Page view(s)
68
checked on Sep 7, 2022
Download(s)
50
checked on Sep 7, 2022
Google ScholarTM
Check
Altmetric
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.