Source:http://linkedlifedata.com/resource/pubmed/id/17204428
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2007-3-26
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pubmed:abstractText |
Thermal dissociation experiments, implemented with blackbody infrared radiative dissociation and Fourier-transform ion cyclotron resonance mass spectrometry, are performed on gaseous protonated and deprotonated ions of the homopentameric B subunits of Shiga toxin 1 (Stx1 B5) and Shiga toxin 2 (Stx2 B5) and the homotetramer streptavidin (S4). Dissociation of the gaseous, multisubunit complexes proceeds predominantly by the loss of a single subunit. Notably, the fractional partitioning of charge between the product ions, i.e., the leaving subunit and the resulting multimer, for a given complex is, within error, constant over the range of charge states investigated. The Arrhenius activation parameters (E(a), A) measured for the loss of subunit decrease with increasing charge state of the complex. However, the parameters for the protonated and deprotonated ions, with the same number of charges, are indistinguishable. The influence of the complex charge state on the dissociation pathways and the magnitude of the dissociation E(a) are modeled theoretically with the discrete charge droplet model (DCDM) and the protein structure model (PSM), wherein the structure of the subunits is considered. Importantly, the major subunit charge states observed experimentally for the Stx1 B5(n+/-) ions correspond to the minimum energy charge distribution predicted by DCDM and PSM assuming a late dissociative transition-state (TS); while for structurally-related Stx2 B5(n+) ions, the experimental charge distribution corresponds to an early TS. It is proposed that the lateness of the TS is related, in part, to the degree of unfolding of the leaving subunit, with Stx1 B being more unfolded than Stx2 B. PSM, incorporating significant subunit unfolding is necessary to account for the product ions observed for the S4(n+) ions. The contribution of Coulombic repulsion to the dissociation E(a) is quantified and the intrinsic activation energy is estimated for the first time.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Gases,
http://linkedlifedata.com/resource/pubmed/chemical/Ions,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Protons,
http://linkedlifedata.com/resource/pubmed/chemical/Shiga Toxin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Shiga Toxin 2,
http://linkedlifedata.com/resource/pubmed/chemical/Streptavidin
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1044-0305
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
617-31
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:17204428-Gases,
pubmed-meshheading:17204428-Hot Temperature,
pubmed-meshheading:17204428-Ions,
pubmed-meshheading:17204428-Multiprotein Complexes,
pubmed-meshheading:17204428-Protons,
pubmed-meshheading:17204428-Shiga Toxin 1,
pubmed-meshheading:17204428-Shiga Toxin 2,
pubmed-meshheading:17204428-Spectroscopy, Fourier Transform Infrared,
pubmed-meshheading:17204428-Streptavidin
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pubmed:year |
2007
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pubmed:articleTitle |
Influence of Coulombic repulsion on the dissociation pathways and energetics of multiprotein complexes in the gas phase.
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pubmed:affiliation |
Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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