ArticleJournal of the American Society for Mass Spectrometry2014
Surface induced dissociation yields quaternary substructure of refractory noncovalent phosphorylase B and glutamate dehydrogenase complexes.
Article in Journal of the American Society for Mass Spectrometry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 42 citations in OpenAlex.
- Oxidized and Reduced Dimeric Protein Complexes Illustrate Contrasting CID and SID Charge Partitioning.Journal of the American Society for Mass Spectrometry · 2023Article
- Simulation of Energy-Resolved Mass Spectrometry Distributions from Surface-Induced Dissociation.Analytical chemistry · 2022Article
- Symmetry of 4-Oxalocrotonate Tautomerase Trimers Influences Unfolding and Fragmentation in the Gas Phase.Journal of the American Chemical Society · 2022Article
- Approaches to Heterogeneity in Native Mass Spectrometry.Chemical reviews · 2022Review
- Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool.Chemical reviews · 2022Review
- Investigation of Charge-State-Dependent Compaction of Protein Ions with Native Ion Mobility-Mass Spectrometry and Theory.Journal of the American Society for Mass Spectrometry · 2022Article
- Surface-induced dissociation of protein complexes on a cyclic ion mobility spectrometer.The Analyst · 2021Article
- Surface-Induced Dissociation of Protein Complexes Selected by Trapped Ion Mobility Spectrometry.Analytical chemistry · 2021Article
- Tandem surface-induced dissociation of protein complexes on an ultrahigh resolution platform.International journal of mass spectrometry · 2021Article
- Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry.Chemical science · 2020Review
- Simple and Minimally Invasive SID Devices for Native Mass Spectrometry.Analytical chemistry · 2020Article
- Population Distributions from Native Mass Spectrometry Titrations Reveal Nearest-Neighbor Cooperativity in the Ring-Shaped Oligomeric Protein TRAP.Biochemistry · 2020Article
- Ion Mobility and Surface Collisions: Submicrometer Capillaries Can Produce Native-like Protein Complexes.Analytical chemistry · 2020Article
- Ion Activation Methods for Peptides and Proteins.Analytical chemistry · 2020Review
- Design and Performance of a Second-Generation Surface-Induced Dissociation Cell for Fourier Transform Ion Cyclotron Resonance Mass Spectrometry of Native Protein Complexes.Analytical chemistry · 2019Article
- Predicting Protein Complex Structure from Surface-Induced Dissociation Mass Spectrometry Data.ACS central science · 2019Article
- Experimental and theoretical investigation of overall energy deposition in surface-induced unfolding of protein ions.Chemical science · 2019Article
- Surface-Induced Dissociation of Noncovalent Protein Complexes in an Extended Mass Range Orbitrap Mass Spectrometer.Analytical chemistry · 2019Article
- Conditions for Analysis of Native Protein Structures Using Uniform Field Drift Tube Ion Mobility Mass Spectrometry and Characterization of Stable Calibrants for TWIM-MS.Journal of the American Society for Mass Spectrometry · 2019Article
- Surface-Induced Dissociation: An Effective Method for Characterization of Protein Quaternary Structure.Analytical chemistry · 2019Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ion mobility (IM) and tandem mass spectrometry (MS/MS) coupled with native MS are useful for studying noncovalent protein complexes. Collision induced dissociation (CID) is the most common MS/MS dissociation method. However, some protein complexes, including glycogen phosphorylase B kinase (PHB) and L-glutamate dehydrogenase (GDH) examined in this study, are resistant to dissociation by CID at the maximum collision energy available in the instrument. Surface induced dissociation (SID) was applied to dissociate the two refractory protein complexes. Different charge state precursor ions of the two complexes were examined by CID and SID. The PHB dimer was successfully dissociated to monomers and the GDH hexamer formed trimeric subcomplexes that are informative of its quaternary structure. The unfolding of the precursor and the percentages of the distinct products suggest that the dissociation pathways vary for different charge states. The precursors at lower charge states (+21 for PHB dimer and +27 for GDH hexamer) produce a higher percentage of folded fragments and dissociate more symmetrically than the precusors at higher charge states (+29 for PHB dimer and +39 for GDH hexamer). The precursors at lower charge state may be more native-like than the higher charge state because a higher percentage of folded fragments and a lower percentage of highly charged unfolded fragments are detected. The combination of SID and charge reduction is shown to be a powerful tool for quaternary structure analysis of refractory noncovalent protein complexes, as illustrated by the data for PHB dimer and GDH hexamer.
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