Native Electrospray and Electron-Capture Dissociation FTICR Mass Spectrometry for Top-Down Studies of Protein Assemblies

The high sensitivity, extended mass range, and fast data acquisition/processing of mass spectrometry and its coupling with native electrospray ionization (ESI) make the combination complementary to other biophysical methods of protein analysis. Protein assemblies with molecular masses up to MDa are...

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Veröffentlicht in:Analytical chemistry (Washington) 2011-07, Vol.83 (14), p.5598-5606
Hauptverfasser: Zhang, Hao, Cui, Weidong, Wen, Jianzhong, Blankenship, Robert E, Gross, Michael L
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container_issue 14
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creator Zhang, Hao
Cui, Weidong
Wen, Jianzhong
Blankenship, Robert E
Gross, Michael L
description The high sensitivity, extended mass range, and fast data acquisition/processing of mass spectrometry and its coupling with native electrospray ionization (ESI) make the combination complementary to other biophysical methods of protein analysis. Protein assemblies with molecular masses up to MDa are now accessible by this approach. Most current approaches have used quadrupole/time-of-flight tandem mass spectrometry, sometimes coupled with ion mobility, to reveal stoichiometry, shape, and dissociation of protein assemblies. The amino-acid sequence of the subunits, however, still relies heavily on independent bottom-up proteomics. We describe here an approach to study protein assemblies that integrates electron-capture dissociation (ECD), native ESI, and FTICR mass spectrometry (12 T). Flexible regions of assembly subunits of yeast alcohol dehydrogenase (147 kDa), concanavalin A (103 kDa), and photosynthetic Fenna–Matthews–Olson antenna protein complex (140 kDa) can be sequenced by ECD or “activated-ion” ECD. Furthermore, noncovalent metal-binding sites can also be determined for the concanavalin A assembly. Most importantly, the regions that undergo fragmentation, either from one of the termini by ECD or from the middle of a protein, as initiated by CID, correlate well with the B-factor from X-ray crystallography of that protein. This factor is a measure of the extent an atom can move from its coordinated position as a function of temperature or crystal imperfections. The approach provides not only top-down proteomics information of the complex subunits but also structural insights complementary to those obtained by ion mobility.
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Psychology ; Light-Harvesting Protein Complexes - chemistry ; Mass spectrometry ; Mass Spectrometry - instrumentation ; Mass Spectrometry - methods ; Models, Molecular ; Molecular and cellular biology ; Molecular Sequence Data ; Plant Proteins - chemistry ; Proteins ; Proteins - chemistry ; Saccharomyces cerevisiae - enzymology ; solar (fuels), photosynthesis (natural and artificial), biofuels (including algae and biomass), bio-inspired, charge transport, membrane, synthesis (novel materials), synthesis (self-assembly) ; Spectrometric and optical methods ; Spectrometry, Mass, Electrospray Ionization - instrumentation ; Spectrometry, Mass, Electrospray Ionization - methods</subject><ispartof>Analytical chemistry (Washington), 2011-07, Vol.83 (14), p.5598-5606</ispartof><rights>Copyright © 2011 American Chemical Society</rights><rights>2015 INIST-CNRS</rights><rights>Copyright American Chemical Society Jul 15, 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a554t-6c8d3f28f26737bce47e5f981d9b4fe02abf734781d74bd451473c71113eb52a3</citedby><cites>FETCH-LOGICAL-a554t-6c8d3f28f26737bce47e5f981d9b4fe02abf734781d74bd451473c71113eb52a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/ac200695d$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ac200695d$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,780,784,885,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=24339908$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21612283$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1065573$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Hao</creatorcontrib><creatorcontrib>Cui, Weidong</creatorcontrib><creatorcontrib>Wen, Jianzhong</creatorcontrib><creatorcontrib>Blankenship, Robert E</creatorcontrib><creatorcontrib>Gross, Michael L</creatorcontrib><creatorcontrib>Energy Frontier Research Centers (EFRC)</creatorcontrib><creatorcontrib>Photosynthetic Antenna Research Center (PARC)</creatorcontrib><title>Native Electrospray and Electron-Capture Dissociation FTICR Mass Spectrometry for Top-Down Studies of Protein Assemblies</title><title>Analytical chemistry (Washington)</title><addtitle>Anal. Chem</addtitle><description>The high sensitivity, extended mass range, and fast data acquisition/processing of mass spectrometry and its coupling with native electrospray ionization (ESI) make the combination complementary to other biophysical methods of protein analysis. Protein assemblies with molecular masses up to MDa are now accessible by this approach. Most current approaches have used quadrupole/time-of-flight tandem mass spectrometry, sometimes coupled with ion mobility, to reveal stoichiometry, shape, and dissociation of protein assemblies. The amino-acid sequence of the subunits, however, still relies heavily on independent bottom-up proteomics. We describe here an approach to study protein assemblies that integrates electron-capture dissociation (ECD), native ESI, and FTICR mass spectrometry (12 T). Flexible regions of assembly subunits of yeast alcohol dehydrogenase (147 kDa), concanavalin A (103 kDa), and photosynthetic Fenna–Matthews–Olson antenna protein complex (140 kDa) can be sequenced by ECD or “activated-ion” ECD. Furthermore, noncovalent metal-binding sites can also be determined for the concanavalin A assembly. Most importantly, the regions that undergo fragmentation, either from one of the termini by ECD or from the middle of a protein, as initiated by CID, correlate well with the B-factor from X-ray crystallography of that protein. This factor is a measure of the extent an atom can move from its coordinated position as a function of temperature or crystal imperfections. 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Chem</addtitle><date>2011-07-15</date><risdate>2011</risdate><volume>83</volume><issue>14</issue><spage>5598</spage><epage>5606</epage><pages>5598-5606</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>The high sensitivity, extended mass range, and fast data acquisition/processing of mass spectrometry and its coupling with native electrospray ionization (ESI) make the combination complementary to other biophysical methods of protein analysis. Protein assemblies with molecular masses up to MDa are now accessible by this approach. Most current approaches have used quadrupole/time-of-flight tandem mass spectrometry, sometimes coupled with ion mobility, to reveal stoichiometry, shape, and dissociation of protein assemblies. The amino-acid sequence of the subunits, however, still relies heavily on independent bottom-up proteomics. We describe here an approach to study protein assemblies that integrates electron-capture dissociation (ECD), native ESI, and FTICR mass spectrometry (12 T). Flexible regions of assembly subunits of yeast alcohol dehydrogenase (147 kDa), concanavalin A (103 kDa), and photosynthetic Fenna–Matthews–Olson antenna protein complex (140 kDa) can be sequenced by ECD or “activated-ion” ECD. Furthermore, noncovalent metal-binding sites can also be determined for the concanavalin A assembly. Most importantly, the regions that undergo fragmentation, either from one of the termini by ECD or from the middle of a protein, as initiated by CID, correlate well with the B-factor from X-ray crystallography of that protein. This factor is a measure of the extent an atom can move from its coordinated position as a function of temperature or crystal imperfections. The approach provides not only top-down proteomics information of the complex subunits but also structural insights complementary to those obtained by ion mobility.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>21612283</pmid><doi>10.1021/ac200695d</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record>
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subjects Alcohol Dehydrogenase - chemistry
Amino Acid Sequence
Amino acids
Analytical chemistry
Bacterial Proteins - chemistry
BASIC BIOLOGICAL SCIENCES
Binding sites
Biological and medical sciences
Canavalia - chemistry
Chemistry
Chlorobi - chemistry
Concanavalin A - chemistry
Crystallography
Diverse techniques
Electrons
Equipment Design
Exact sciences and technology
Fourier Analysis
Fundamental and applied biological sciences. Psychology
Light-Harvesting Protein Complexes - chemistry
Mass spectrometry
Mass Spectrometry - instrumentation
Mass Spectrometry - methods
Models, Molecular
Molecular and cellular biology
Molecular Sequence Data
Plant Proteins - chemistry
Proteins
Proteins - chemistry
Saccharomyces cerevisiae - enzymology
solar (fuels), photosynthesis (natural and artificial), biofuels (including algae and biomass), bio-inspired, charge transport, membrane, synthesis (novel materials), synthesis (self-assembly)
Spectrometric and optical methods
Spectrometry, Mass, Electrospray Ionization - instrumentation
Spectrometry, Mass, Electrospray Ionization - methods
title Native Electrospray and Electron-Capture Dissociation FTICR Mass Spectrometry for Top-Down Studies of Protein Assemblies
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