Infrared Multiphoton Dissociation of Peptide Cations in a Dual Pressure Linear Ion Trap Mass Spectrometer
A dual pressure linear ion trap mass spectrometer was modified to permit infrared multiphoton dissociation (IRMPD) in each of the two cellsthe first a high pressure cell operated at nominally 5 × 10−3 Torr and the second a low pressure cell operated at nominally 3 × 10−4 Torr. When IRMPD was perfor...
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creator | Gardner, Myles W. Smith, Suncerae I. Ledvina, Aaron R. Madsen, James A. Coon, Joshua J. Schwartz, Jae C. Stafford, George C. Brodbelt, Jennifer S. |
description | A dual pressure linear ion trap mass spectrometer was modified to permit infrared multiphoton dissociation (IRMPD) in each of the two cellsthe first a high pressure cell operated at nominally 5 × 10−3 Torr and the second a low pressure cell operated at nominally 3 × 10−4 Torr. When IRMPD was performed in the high pressure cell, most peptide ions did not undergo significant photodissociation; however, in the low pressure cell peptide cations were efficiently dissociated with less than 25 ms of IR irradiation regardless of charge state. IRMPD of peptide cations allowed the detection of low m/z product ions including the y1 fragments and immonium ions which are not typically observed by ion trap collision induced dissociation (CID). Photodissociation efficiencies of ∼100% and MS/MS (tandem mass spectrometry) efficiencies of greater than 60% were observed for both multiply and singly protonated peptides. In general, higher sequence coverage of peptides was obtained using IRMPD over CID. Further, greater than 90% of the product ion current in the IRMPD mass spectra of doubly charged peptide ions was composed of singly charged product ions compared to the CID mass spectra in which the abundances of the multiply and singly charged product ions were equally divided. Highly charged primary product ions also underwent efficient photodissociation to yield singly charged secondary product ions, thus simplifying the IRMPD product ion mass spectra. |
doi_str_mv | 10.1021/ac901313m |
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When IRMPD was performed in the high pressure cell, most peptide ions did not undergo significant photodissociation; however, in the low pressure cell peptide cations were efficiently dissociated with less than 25 ms of IR irradiation regardless of charge state. IRMPD of peptide cations allowed the detection of low m/z product ions including the y1 fragments and immonium ions which are not typically observed by ion trap collision induced dissociation (CID). Photodissociation efficiencies of ∼100% and MS/MS (tandem mass spectrometry) efficiencies of greater than 60% were observed for both multiply and singly protonated peptides. In general, higher sequence coverage of peptides was obtained using IRMPD over CID. Further, greater than 90% of the product ion current in the IRMPD mass spectra of doubly charged peptide ions was composed of singly charged product ions compared to the CID mass spectra in which the abundances of the multiply and singly charged product ions were equally divided. Highly charged primary product ions also underwent efficient photodissociation to yield singly charged secondary product ions, thus simplifying the IRMPD product ion mass spectra.</description><identifier>ISSN: 0003-2700</identifier><identifier>EISSN: 1520-6882</identifier><identifier>DOI: 10.1021/ac901313m</identifier><identifier>PMID: 19739654</identifier><identifier>CODEN: ANCHAM</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Amino Acid Sequence ; Analytical chemistry ; Cations - chemistry ; Cells ; Chemistry ; Exact sciences and technology ; Infrared radiation ; Infrared Rays ; Ions ; Mass spectrometry ; Molecular Sequence Data ; Peptides ; Peptides - chemistry ; Spectrometric and optical methods ; Tandem Mass Spectrometry - instrumentation ; Tandem Mass Spectrometry - methods</subject><ispartof>Analytical chemistry (Washington), 2009-10, Vol.81 (19), p.8109-8118</ispartof><rights>Copyright © 2009 American Chemical Society</rights><rights>2015 INIST-CNRS</rights><rights>Copyright American Chemical Society Oct 1, 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a461t-f9412e6a1c04908a9c59790a05e2706087b2a6442431622a1691c30d678084ce3</citedby><cites>FETCH-LOGICAL-a461t-f9412e6a1c04908a9c59790a05e2706087b2a6442431622a1691c30d678084ce3</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/ac901313m$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ac901313m$$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&idt=22062821$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19739654$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gardner, Myles W.</creatorcontrib><creatorcontrib>Smith, Suncerae I.</creatorcontrib><creatorcontrib>Ledvina, Aaron R.</creatorcontrib><creatorcontrib>Madsen, James A.</creatorcontrib><creatorcontrib>Coon, Joshua J.</creatorcontrib><creatorcontrib>Schwartz, Jae C.</creatorcontrib><creatorcontrib>Stafford, George C.</creatorcontrib><creatorcontrib>Brodbelt, Jennifer S.</creatorcontrib><title>Infrared Multiphoton Dissociation of Peptide Cations in a Dual Pressure Linear Ion Trap Mass Spectrometer</title><title>Analytical chemistry (Washington)</title><addtitle>Anal. Chem</addtitle><description>A dual pressure linear ion trap mass spectrometer was modified to permit infrared multiphoton dissociation (IRMPD) in each of the two cellsthe first a high pressure cell operated at nominally 5 × 10−3 Torr and the second a low pressure cell operated at nominally 3 × 10−4 Torr. When IRMPD was performed in the high pressure cell, most peptide ions did not undergo significant photodissociation; however, in the low pressure cell peptide cations were efficiently dissociated with less than 25 ms of IR irradiation regardless of charge state. IRMPD of peptide cations allowed the detection of low m/z product ions including the y1 fragments and immonium ions which are not typically observed by ion trap collision induced dissociation (CID). Photodissociation efficiencies of ∼100% and MS/MS (tandem mass spectrometry) efficiencies of greater than 60% were observed for both multiply and singly protonated peptides. In general, higher sequence coverage of peptides was obtained using IRMPD over CID. Further, greater than 90% of the product ion current in the IRMPD mass spectra of doubly charged peptide ions was composed of singly charged product ions compared to the CID mass spectra in which the abundances of the multiply and singly charged product ions were equally divided. Highly charged primary product ions also underwent efficient photodissociation to yield singly charged secondary product ions, thus simplifying the IRMPD product ion mass spectra.</description><subject>Amino Acid Sequence</subject><subject>Analytical chemistry</subject><subject>Cations - chemistry</subject><subject>Cells</subject><subject>Chemistry</subject><subject>Exact sciences and technology</subject><subject>Infrared radiation</subject><subject>Infrared Rays</subject><subject>Ions</subject><subject>Mass spectrometry</subject><subject>Molecular Sequence Data</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Spectrometric and optical methods</subject><subject>Tandem Mass Spectrometry - instrumentation</subject><subject>Tandem Mass Spectrometry - methods</subject><issn>0003-2700</issn><issn>1520-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNplkVtr3DAQhUVpaLZpH_oHiiiE0ge3M7JWtl8KZdPLwoYGmj6LiXbcKNiWI9mB_vsqzbLbC3oQmvl05gxHiBcIbxEUviPXAJZY9o_EApcKClPX6rFYAEBZqArgWDxN6QYAEdA8EcfYVGVjlnoh_HpoI0XeyvO5m_x4HaYwyDOfUnCeJp8foZUXPE5-y3L1u5KkHyTJs5k6eRE5pTmy3PiBKcp1_nAZaZTnlJL8NrKbYuh54vhMHLXUJX6-u0_E908fL1dfis3Xz-vVh01B2uBUtI1GxYbQgW6gpsYtm6oBgiXnTQzU1ZUio7XSJRqlCE2DroStqWqotePyRLx_0B3nq563jocpUmfH6HuKP20gb__uDP7a_gh3VlWVzicLvN4JxHA7c5ps75PjrqOBw5xsVWoweX6dyVf_kDdhjkPezirMpqGsMENvHiAXQ0qR270VBHsfn93Hl9mXf3o_kLu8MnC6Ayg56nJ0g_NpzykFRtUKDxy5dDD1_8BfReOtAg</recordid><startdate>20091001</startdate><enddate>20091001</enddate><creator>Gardner, Myles W.</creator><creator>Smith, Suncerae I.</creator><creator>Ledvina, Aaron R.</creator><creator>Madsen, James A.</creator><creator>Coon, Joshua J.</creator><creator>Schwartz, Jae C.</creator><creator>Stafford, George C.</creator><creator>Brodbelt, Jennifer S.</creator><general>American Chemical Society</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U7</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20091001</creationdate><title>Infrared Multiphoton Dissociation of Peptide Cations in a Dual Pressure Linear Ion Trap Mass Spectrometer</title><author>Gardner, Myles W. ; Smith, Suncerae I. ; Ledvina, Aaron R. ; Madsen, James A. ; Coon, Joshua J. ; Schwartz, Jae C. ; Stafford, George C. ; Brodbelt, Jennifer S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a461t-f9412e6a1c04908a9c59790a05e2706087b2a6442431622a1691c30d678084ce3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical chemistry</topic><topic>Cations - chemistry</topic><topic>Cells</topic><topic>Chemistry</topic><topic>Exact sciences and technology</topic><topic>Infrared radiation</topic><topic>Infrared Rays</topic><topic>Ions</topic><topic>Mass spectrometry</topic><topic>Molecular Sequence Data</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Spectrometric and optical methods</topic><topic>Tandem Mass Spectrometry - instrumentation</topic><topic>Tandem Mass Spectrometry - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gardner, Myles W.</creatorcontrib><creatorcontrib>Smith, Suncerae I.</creatorcontrib><creatorcontrib>Ledvina, Aaron R.</creatorcontrib><creatorcontrib>Madsen, James A.</creatorcontrib><creatorcontrib>Coon, Joshua J.</creatorcontrib><creatorcontrib>Schwartz, Jae C.</creatorcontrib><creatorcontrib>Stafford, George C.</creatorcontrib><creatorcontrib>Brodbelt, Jennifer S.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Analytical chemistry (Washington)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gardner, Myles W.</au><au>Smith, Suncerae I.</au><au>Ledvina, Aaron R.</au><au>Madsen, James A.</au><au>Coon, Joshua J.</au><au>Schwartz, Jae C.</au><au>Stafford, George C.</au><au>Brodbelt, Jennifer S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Infrared Multiphoton Dissociation of Peptide Cations in a Dual Pressure Linear Ion Trap Mass Spectrometer</atitle><jtitle>Analytical chemistry (Washington)</jtitle><addtitle>Anal. Chem</addtitle><date>2009-10-01</date><risdate>2009</risdate><volume>81</volume><issue>19</issue><spage>8109</spage><epage>8118</epage><pages>8109-8118</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>A dual pressure linear ion trap mass spectrometer was modified to permit infrared multiphoton dissociation (IRMPD) in each of the two cellsthe first a high pressure cell operated at nominally 5 × 10−3 Torr and the second a low pressure cell operated at nominally 3 × 10−4 Torr. When IRMPD was performed in the high pressure cell, most peptide ions did not undergo significant photodissociation; however, in the low pressure cell peptide cations were efficiently dissociated with less than 25 ms of IR irradiation regardless of charge state. IRMPD of peptide cations allowed the detection of low m/z product ions including the y1 fragments and immonium ions which are not typically observed by ion trap collision induced dissociation (CID). Photodissociation efficiencies of ∼100% and MS/MS (tandem mass spectrometry) efficiencies of greater than 60% were observed for both multiply and singly protonated peptides. In general, higher sequence coverage of peptides was obtained using IRMPD over CID. Further, greater than 90% of the product ion current in the IRMPD mass spectra of doubly charged peptide ions was composed of singly charged product ions compared to the CID mass spectra in which the abundances of the multiply and singly charged product ions were equally divided. Highly charged primary product ions also underwent efficient photodissociation to yield singly charged secondary product ions, thus simplifying the IRMPD product ion mass spectra.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>19739654</pmid><doi>10.1021/ac901313m</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Analytical chemistry Cations - chemistry Cells Chemistry Exact sciences and technology Infrared radiation Infrared Rays Ions Mass spectrometry Molecular Sequence Data Peptides Peptides - chemistry Spectrometric and optical methods Tandem Mass Spectrometry - instrumentation Tandem Mass Spectrometry - methods |
title | Infrared Multiphoton Dissociation of Peptide Cations in a Dual Pressure Linear Ion Trap Mass Spectrometer |
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