View in EDS

Tandem surface-induced dissociation of protein complexes on an ultrahigh resolution platform.

Saved in:
Bibliographic Details
Title: Tandem surface-induced dissociation of protein complexes on an ultrahigh resolution platform.
Authors: Snyder, Dalton T.1 (AUTHOR), Lin, Yu-Fu1,2 (AUTHOR), Somogyi, Arpad1 (AUTHOR), Wysocki, Vicki H.1,2 (AUTHOR) wysocki.11@osu.edu
Source: International Journal of Mass Spectrometry. Mar2021, Vol. 461, pN.PAG-N.PAG. 1p.
Subjects: Cyclotron resonance, Daughter ions, Mass spectrometers, Proteins, Fourier transforms
Abstract: We describe instrumentation for conducting tandem surface-induced dissociation (tSID) of native protein complexes on an ultrahigh resolution Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometer. The two stages of SID are accomplished with split lenses replacing the entrance lenses of the quadrupole mass filter (stage 1, referred to herein as SID-Q) and the collision cell (stage 2, Q-SID). After SID-Q, the scattered projectile ions and subcomplexes formed in transit traverse the pre-filter prior to the mass-selecting quadrupole, providing preliminary insights into the SID fragmentation kinetics of noncovalent protein complexes. The isolated SID fragments (subcomplexes) are then fragmented by SID in the collision cell entrance lens (Q-SID), generating subcomplexes of subcomplexes. We show that the ultrahigh resolution of the FT-ICR can be used for deconvolving species overlapping in m/z, which are particularly prominent in tandem SID spectra due to the combination of symmetric charge partitioning and narrow product ion charge state distributions. Various protein complex topologies are explored, including homotetramers, homopentamers, a homohexamer, and a heterohexamer. Image 1 • Tandem SID designs are described for FT-ICR and Q-IM-TOF platforms. • Tandem SID of protein complexes reveals subunit connectivity. • Ultrahigh resolution FT-ICR deconvolves overlapping charge states. [ABSTRACT FROM AUTHOR]
Copyright of International Journal of Mass Spectrometry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
FullText Text:
  Availability: 0
Header DbId: egs
DbLabel: Engineering Source
An: 148385223
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Tandem surface-induced dissociation of protein complexes on an ultrahigh resolution platform.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Snyder%2C+Dalton+T%2E%22">Snyder, Dalton T.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Lin%2C+Yu-Fu%22">Lin, Yu-Fu</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Somogyi%2C+Arpad%22">Somogyi, Arpad</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Wysocki%2C+Vicki+H%2E%22">Wysocki, Vicki H.</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<i> wysocki.11@osu.edu</i>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22International+Journal+of+Mass+Spectrometry%22">International Journal of Mass Spectrometry</searchLink>. Mar2021, Vol. 461, pN.PAG-N.PAG. 1p.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Cyclotron+resonance%22">Cyclotron resonance</searchLink><br /><searchLink fieldCode="DE" term="%22Daughter+ions%22">Daughter ions</searchLink><br /><searchLink fieldCode="DE" term="%22Mass+spectrometers%22">Mass spectrometers</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Fourier+transforms%22">Fourier transforms</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: We describe instrumentation for conducting tandem surface-induced dissociation (tSID) of native protein complexes on an ultrahigh resolution Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometer. The two stages of SID are accomplished with split lenses replacing the entrance lenses of the quadrupole mass filter (stage 1, referred to herein as SID-Q) and the collision cell (stage 2, Q-SID). After SID-Q, the scattered projectile ions and subcomplexes formed in transit traverse the pre-filter prior to the mass-selecting quadrupole, providing preliminary insights into the SID fragmentation kinetics of noncovalent protein complexes. The isolated SID fragments (subcomplexes) are then fragmented by SID in the collision cell entrance lens (Q-SID), generating subcomplexes of subcomplexes. We show that the ultrahigh resolution of the FT-ICR can be used for deconvolving species overlapping in m/z, which are particularly prominent in tandem SID spectra due to the combination of symmetric charge partitioning and narrow product ion charge state distributions. Various protein complex topologies are explored, including homotetramers, homopentamers, a homohexamer, and a heterohexamer. Image 1 • Tandem SID designs are described for FT-ICR and Q-IM-TOF platforms. • Tandem SID of protein complexes reveals subunit connectivity. • Ultrahigh resolution FT-ICR deconvolves overlapping charge states. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of International Journal of Mass Spectrometry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=148385223
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1016/j.ijms.2020.116503
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 1
        StartPage: N.PAG
    Subjects:
      – SubjectFull: Cyclotron resonance
        Type: general
      – SubjectFull: Daughter ions
        Type: general
      – SubjectFull: Mass spectrometers
        Type: general
      – SubjectFull: Proteins
        Type: general
      – SubjectFull: Fourier transforms
        Type: general
    Titles:
      – TitleFull: Tandem surface-induced dissociation of protein complexes on an ultrahigh resolution platform.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Snyder, Dalton T.
      – PersonEntity:
          Name:
            NameFull: Lin, Yu-Fu
      – PersonEntity:
          Name:
            NameFull: Somogyi, Arpad
      – PersonEntity:
          Name:
            NameFull: Wysocki, Vicki H.
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 03
              Text: Mar2021
              Type: published
              Y: 2021
          Identifiers:
            – Type: issn-print
              Value: 13873806
          Numbering:
            – Type: volume
              Value: 461
          Titles:
            – TitleFull: International Journal of Mass Spectrometry
              Type: main
ResultId 1