Top-Down Protein Fragmentation by Infrared Multiphoton Dissociation in a Dual Pressure Linear Ion Trap
Infrared multiphoton dissociation (IRMPD) was implemented in a novel dual pressure linear ion trap for rapid top-down proteomics. The high pressure cell provided improved trapping and isolation efficiencies while the isotopic profiles of 10+ charged ions could be resolved by mass analysis in the low...
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| Veröffentlicht in: | Analytical chemistry (Washington) 2009-11, Vol.81 (21), p.8677-8686 |
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| container_title | Analytical chemistry (Washington) |
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| creator | Madsen, James A Gardner, Myles W Smith, Suncerae I Ledvina, Aaron R Coon, Joshua J Schwartz, Jae C Stafford, George C Brodbelt, Jennifer S |
| description | Infrared multiphoton dissociation (IRMPD) was implemented in a novel dual pressure linear ion trap for rapid top-down proteomics. The high pressure cell provided improved trapping and isolation efficiencies while the isotopic profiles of 10+ charged ions could be resolved by mass analysis in the low pressure cell that enabled effective top down protein identification. Striking differences between IRMPD in the low pressure cell and CID in the high pressure cell were observed for proteins ranging from 8.6 to 29 kDa. Because of secondary dissociation, IRMPD yielded product ions in significantly lower charge states as compared to CID, thus facilitating more accurate mass identification and streamlining product ion assignment. This outcome was especially useful for database searching of larger proteins (∼29 kDa) as IRMPD substantially improved protein identification and scoring confidence. Also, IRMPD showed an increased selectivity toward backbone cleavages N-terminal to proline and C-terminal to acidic residues (especially for the lowest charge states), which could be useful for a priori spectral predictions and enhanced database searching for protein identification. |
| doi_str_mv | 10.1021/ac901554z |
| format | Article |
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Gardner, Myles W ; Smith, Suncerae I ; Ledvina, Aaron R ; Coon, Joshua J ; Schwartz, Jae C ; Stafford, George C ; Brodbelt, Jennifer S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a371t-9409e426b5712938e7dc8aefd7e64710ca3c4a427293dfc3244b3956421d1f733</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Analytical chemistry</topic><topic>Biochemistry</topic><topic>Cells</topic><topic>Chemistry</topic><topic>Databases, Protein</topic><topic>Exact sciences and technology</topic><topic>Infrared Rays</topic><topic>Ion Transport</topic><topic>Ions</topic><topic>Ions - chemistry</topic><topic>Pressure</topic><topic>Proline - chemistry</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Proteomics</topic><topic>Proteomics - instrumentation</topic><topic>Proteomics - methods</topic><topic>Spectrometric and optical methods</topic><topic>Tandem Mass Spectrometry - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Madsen, James A</creatorcontrib><creatorcontrib>Gardner, Myles W</creatorcontrib><creatorcontrib>Smith, Suncerae I</creatorcontrib><creatorcontrib>Ledvina, Aaron R</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><jtitle>Analytical chemistry (Washington)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Madsen, James A</au><au>Gardner, Myles W</au><au>Smith, Suncerae I</au><au>Ledvina, Aaron R</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>Top-Down Protein Fragmentation by Infrared Multiphoton Dissociation in a Dual Pressure Linear Ion Trap</atitle><jtitle>Analytical chemistry (Washington)</jtitle><addtitle>Anal. Chem</addtitle><date>2009-11-01</date><risdate>2009</risdate><volume>81</volume><issue>21</issue><spage>8677</spage><epage>8686</epage><pages>8677-8686</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>Infrared multiphoton dissociation (IRMPD) was implemented in a novel dual pressure linear ion trap for rapid top-down proteomics. The high pressure cell provided improved trapping and isolation efficiencies while the isotopic profiles of 10+ charged ions could be resolved by mass analysis in the low pressure cell that enabled effective top down protein identification. Striking differences between IRMPD in the low pressure cell and CID in the high pressure cell were observed for proteins ranging from 8.6 to 29 kDa. Because of secondary dissociation, IRMPD yielded product ions in significantly lower charge states as compared to CID, thus facilitating more accurate mass identification and streamlining product ion assignment. 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| ispartof | Analytical chemistry (Washington), 2009-11, Vol.81 (21), p.8677-8686 |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Analytical chemistry Biochemistry Cells Chemistry Databases, Protein Exact sciences and technology Infrared Rays Ion Transport Ions Ions - chemistry Pressure Proline - chemistry Proteins Proteins - chemistry Proteomics Proteomics - instrumentation Proteomics - methods Spectrometric and optical methods Tandem Mass Spectrometry - methods |
| title | Top-Down Protein Fragmentation by Infrared Multiphoton Dissociation in a Dual Pressure Linear Ion Trap |
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