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- W3119086575 endingPage "116503" @default.
- W3119086575 startingPage "116503" @default.
- W3119086575 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 20 mm 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." @default.
- W3119086575 created "2021-01-18" @default.
- W3119086575 creator A5030360815 @default.
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- W3119086575 creator A5070961788 @default.
- W3119086575 date "2021-03-01" @default.
- W3119086575 modified "2023-10-18" @default.
- W3119086575 title "Tandem surface-induced dissociation of protein complexes on an ultrahigh resolution platform" @default.
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- W3119086575 doi "https://doi.org/10.1016/j.ijms.2020.116503" @default.
- W3119086575 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8057730" @default.
- W3119086575 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33889055" @default.
- W3119086575 hasPublicationYear "2021" @default.
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