Please use this identifier to cite or link to this item:
http://hdl.handle.net/1942/23274
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lermyte, Frederik | - |
dc.contributor.author | Łącki, Mateusz Krzysztof | - |
dc.contributor.author | VALKENBORG, Dirk | - |
dc.contributor.author | Gambin, Anna | - |
dc.contributor.author | Sobott, Frank | - |
dc.date.accessioned | 2017-03-02T09:36:33Z | - |
dc.date.available | 2017-03-02T09:36:33Z | - |
dc.date.issued | 2017 | - |
dc.identifier.citation | JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 28(1), p. 69-76 | - |
dc.identifier.issn | 1044-0305 | - |
dc.identifier.uri | http://hdl.handle.net/1942/23274 | - |
dc.description.abstract | Owing to its versatility, electron transfer dissociation (ETD) has become one of the most commonly utilized fragmentation techniques in both native and non-native top-down mass spectrometry. However, several competing reactions-primarily different forms of charge reduction-occur under ETD conditions, as evidenced by the distorted isotope patterns usually observed. In this work, we analyze these isotope patterns to compare the stability of nondissociative electron transfer (ETnoD) products, specifically noncovalent c/z fragment complexes, across a range of ubiquitin conformational states. Using ion mobility, we find that more extended states are more prone to fragment release. We obtain evidence that for a given charge state, populations of ubiquitin ions formed either directly by electrospray ionization or through collapse of more extended states upon charge reduction, span a similar range of collision cross-sections. Products of gas-phase collapse are, however, less stabilized towards unfolding than the native conformation, indicating that the ions retain a memory of previous conformational states. Furthermore, this collapse of charge-reduced ions is promoted if the ions are 'preheated' using collisional activation, with possible implications for the kinetics of gas-phase compaction. | - |
dc.description.sponsorship | The authors thank the Research Foundation - Flanders (FWO) for funding a Ph.D. fellowship (F.L.). The Synapt G2 mass spectrometer is funded by a grant from the Hercules Foundation - Flanders. This work is in part supported by Polish NCN grants no. 2014/12/W/ST5/00592 and 2015/17/N/ST6/03565. | - |
dc.language.iso | en | - |
dc.publisher | SPRINGER | - |
dc.rights | (c) American Society for Mass Spectrometry, 2016 | - |
dc.subject.other | ETD; PTR; Charge reduction; Ion mobility; Protein conformation; Ubiquitin | - |
dc.subject.other | ETD; PTR; charge reduction; ion mobility; protein conformation; ubiquitin | - |
dc.title | Conformational Space and Stability of ETD Charge Reduction Products of Ubiquitin | - |
dc.type | Journal Contribution | - |
local.bibliographicCitation.conferencedate | OCT 16-20, 2015 | - |
local.bibliographicCitation.conferencename | 31st ASMS Asilomar Conference on Native Mass Spectrometry-Based Structural Biology | - |
local.bibliographicCitation.conferenceplace | Pacific Grove, CA | - |
dc.identifier.epage | 76 | - |
dc.identifier.issue | 1 | - |
dc.identifier.spage | 69 | - |
dc.identifier.volume | 28 | - |
local.format.pages | 8 | - |
local.bibliographicCitation.jcat | A1 | - |
dc.description.notes | [Lermyte, Frederik; Sobott, Frank] Univ Antwerp, Dept Chem, Biomol & Analyt Mass Spectrometry Grp, Antwerp, Belgium. [Lermyte, Frederik; Valkenborg, Dirk] Univ Antwerp, Ctr Prote, Antwerp, Belgium. [Lacki, Mateusz Krzysztof; Gambin, Anna] Univ Warsaw, Inst Informat, Warsaw, Poland. [Valkenborg, Dirk] Hasselt Univ, Interuniv Inst Biostat & Stat Bioinformat, Hasselt, Belgium. [Valkenborg, Dirk] Flemish Inst Technol Res VITO, Appl Bio & Mol Syst, Antwerp, Belgium. [Sobott, Frank] Univ Leeds, Astbury Ctr Struct Mol Biol, Leeds LS2 9JT, W Yorkshire, England. [Sobott, Frank] Univ Leeds, Sch Mol & Cellular Biol, Leeds LS2 9JT, W Yorkshire, England. | - |
local.publisher.place | NEW YORK | - |
local.type.refereed | Refereed | - |
local.type.specified | Article | - |
dc.identifier.doi | 10.1007/s13361-016-1444-7 | - |
dc.identifier.isi | 000391433100009 | - |
item.validation | ecoom 2018 | - |
item.accessRights | Restricted Access | - |
item.fullcitation | Lermyte, Frederik; Łącki, Mateusz Krzysztof; VALKENBORG, Dirk; Gambin, Anna & Sobott, Frank (2017) Conformational Space and Stability of ETD Charge Reduction Products of Ubiquitin. In: JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 28(1), p. 69-76. | - |
item.fulltext | With Fulltext | - |
item.contributor | Lermyte, Frederik | - |
item.contributor | Łącki, Mateusz Krzysztof | - |
item.contributor | VALKENBORG, Dirk | - |
item.contributor | Gambin, Anna | - |
item.contributor | Sobott, Frank | - |
crisitem.journal.issn | 1044-0305 | - |
crisitem.journal.eissn | 1879-1123 | - |
Appears in Collections: | Research publications |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
lemyte 1.pdf Restricted Access | Published version | 1.57 MB | Adobe PDF | View/Open Request a copy |
SCOPUSTM
Citations
18
checked on Sep 3, 2020
WEB OF SCIENCETM
Citations
25
checked on May 8, 2024
Page view(s)
62
checked on Sep 7, 2022
Download(s)
48
checked on Sep 7, 2022
Google ScholarTM
Check
Altmetric
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.