Influence of Size on Apparent Scrambling of Sequence During CID of b-Type Ions
We investigated the influence of peptide size on the apparent loss of sequence during collision-induced dissociation (CID) of b ions using a group of peptides containing from between 4 and 10 residues. Although scrambling of sequence for b 3 + generated from tetrapeptides is minimal, significant for...
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| Veröffentlicht in: | Journal of the American Society for Mass Spectrometry 2009-11, Vol.20 (11), p.2174-2181 |
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| creator | Molesworth, Samuel Osburn, Sandra Van Stipdonk, Michael |
| description | We investigated the influence of peptide size on the apparent loss of sequence during collision-induced dissociation (CID) of
b ions using a group of peptides containing from between 4 and 10 residues. Although scrambling of sequence for
b
3
+ generated from tetrapeptides is minimal, significant formation of nondirect sequence ions (i.e., ions for which scrambling has apparently occurred) was observed for all larger
b ions included in the study.
Multiple-stage CID experiments demonstrate loss of internal residues and remarkable similarity of product ion spectra among
b
n
ions from permuted sequence isomers. The results support the hypothesis that significant sequence scrambling can occur following fragmentation of
b-type ions. |
| doi_str_mv | 10.1016/j.jasms.2009.07.023 |
| format | Article |
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b ions using a group of peptides containing from between 4 and 10 residues. Although scrambling of sequence for
b
3
+ generated from tetrapeptides is minimal, significant formation of nondirect sequence ions (i.e., ions for which scrambling has apparently occurred) was observed for all larger
b ions included in the study.
Multiple-stage CID experiments demonstrate loss of internal residues and remarkable similarity of product ion spectra among
b
n
ions from permuted sequence isomers. The results support the hypothesis that significant sequence scrambling can occur following fragmentation of
b-type ions.</description><identifier>ISSN: 1044-0305</identifier><identifier>EISSN: 1879-1123</identifier><identifier>DOI: 10.1016/j.jasms.2009.07.023</identifier><identifier>PMID: 19758821</identifier><language>eng</language><publisher>New York: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Analytical Chemistry ; Analytical, structural and metabolic biochemistry ; Base Sequence ; Bioinformatics ; Biological and medical sciences ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; Fundamental and applied biological sciences. Psychology ; General aspects, investigation methods ; Ions - classification ; Isomerism ; Mass spectrometry ; Molecular Sequence Data ; Molecular Structure ; Oligopeptides - chemical synthesis ; Oligopeptides - chemistry ; Organic Chemistry ; Peptides ; Proteins ; Proteomics ; Residues ; Spectrometry, Mass, Electrospray Ionization</subject><ispartof>Journal of the American Society for Mass Spectrometry, 2009-11, Vol.20 (11), p.2174-2181</ispartof><rights>2009</rights><rights>American Society for Mass Spectrometry 2009</rights><rights>2015 INIST-CNRS</rights><rights>Journal of The American Society for Mass Spectrometry is a copyright of Springer, 2009.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c603t-8685324c8357c6624b5e1338c307cb3b65737c7b2c054334413f899d5248173e3</citedby><cites>FETCH-LOGICAL-c603t-8685324c8357c6624b5e1338c307cb3b65737c7b2c054334413f899d5248173e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1016/j.jasms.2009.07.023$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1016/j.jasms.2009.07.023$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22177627$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19758821$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Molesworth, Samuel</creatorcontrib><creatorcontrib>Osburn, Sandra</creatorcontrib><creatorcontrib>Van Stipdonk, Michael</creatorcontrib><title>Influence of Size on Apparent Scrambling of Sequence During CID of b-Type Ions</title><title>Journal of the American Society for Mass Spectrometry</title><addtitle>J Am Soc Mass Spectrom</addtitle><addtitle>J Am Soc Mass Spectrom</addtitle><description>We investigated the influence of peptide size on the apparent loss of sequence during collision-induced dissociation (CID) of
b ions using a group of peptides containing from between 4 and 10 residues. Although scrambling of sequence for
b
3
+ generated from tetrapeptides is minimal, significant formation of nondirect sequence ions (i.e., ions for which scrambling has apparently occurred) was observed for all larger
b ions included in the study.
Multiple-stage CID experiments demonstrate loss of internal residues and remarkable similarity of product ion spectra among
b
n
ions from permuted sequence isomers. The results support the hypothesis that significant sequence scrambling can occur following fragmentation of
b-type ions.</description><subject>Amino Acid Sequence</subject><subject>Analytical Chemistry</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Base Sequence</subject><subject>Bioinformatics</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects, investigation methods</subject><subject>Ions - classification</subject><subject>Isomerism</subject><subject>Mass spectrometry</subject><subject>Molecular Sequence Data</subject><subject>Molecular Structure</subject><subject>Oligopeptides - chemical synthesis</subject><subject>Oligopeptides - chemistry</subject><subject>Organic Chemistry</subject><subject>Peptides</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Residues</subject><subject>Spectrometry, Mass, Electrospray Ionization</subject><issn>1044-0305</issn><issn>1879-1123</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNkl2L1TAQhoso7of-AkEK4upN6ySTZNKLvVjO-nFg0Ytdr0Obk0pLv0xOhfXXm24PKl4cJBcTJs87M8ybJHnBIGfA1Ls2b8vQh5wDFDlQDhwfJadMU5ExxvFxvIMQGSDIk-QshBaAERT0NDlhBUmtOTtNPm-HupvdYF061ult8zPGIb2aptK7YZ_eWl_2VdcM3x6e3fcVvZ79ktpsr5d0ld3dTy7djkN4ljypyy6454d4nnz98P5u8ym7-fJxu7m6yawC3GdaaYlcWI2SrFJcVNIxRG0RyFZYKUlIlipuQQpEIRjWuih2kgvNCB2eJ2_WupMf40xhb_omWNd15eDGORhCAQXTyCN5cZRECUBCyQi-PQoyRVTEsfV_oFwpkhzk0v7VP2g7zn6IuzGskCye2DpSuFLWjyF4V5vJN33p7w0Ds5htWvNgtlnMNkAmmh1VLw-156p3uz-ag7sReH0AymDLrvblYJvwm-OcESlOkRMrF6bFV-f_GvJo_8tV5qLTP5ooC7ZZ_seu8c7uzW5sjup_ASzH1Ck</recordid><startdate>20091101</startdate><enddate>20091101</enddate><creator>Molesworth, Samuel</creator><creator>Osburn, Sandra</creator><creator>Van Stipdonk, Michael</creator><general>Elsevier Inc</general><general>Springer-Verlag</general><general>Elsevier</general><general>Springer Nature B.V</general><scope>6I.</scope><scope>AAFTH</scope><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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FG</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><scope>7X8</scope></search><sort><creationdate>20091101</creationdate><title>Influence of Size on Apparent Scrambling of Sequence During CID of b-Type Ions</title><author>Molesworth, Samuel ; Osburn, Sandra ; Van Stipdonk, Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c603t-8685324c8357c6624b5e1338c307cb3b65737c7b2c054334413f899d5248173e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical Chemistry</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Base Sequence</topic><topic>Bioinformatics</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects, investigation methods</topic><topic>Ions - classification</topic><topic>Isomerism</topic><topic>Mass spectrometry</topic><topic>Molecular Sequence Data</topic><topic>Molecular Structure</topic><topic>Oligopeptides - chemical synthesis</topic><topic>Oligopeptides - chemistry</topic><topic>Organic Chemistry</topic><topic>Peptides</topic><topic>Proteins</topic><topic>Proteomics</topic><topic>Residues</topic><topic>Spectrometry, Mass, Electrospray Ionization</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Molesworth, Samuel</creatorcontrib><creatorcontrib>Osburn, Sandra</creatorcontrib><creatorcontrib>Van Stipdonk, Michael</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the American Society for Mass Spectrometry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Molesworth, Samuel</au><au>Osburn, Sandra</au><au>Van Stipdonk, Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Influence of Size on Apparent Scrambling of Sequence During CID of b-Type Ions</atitle><jtitle>Journal of the American Society for Mass Spectrometry</jtitle><stitle>J Am Soc Mass Spectrom</stitle><addtitle>J Am Soc Mass Spectrom</addtitle><date>2009-11-01</date><risdate>2009</risdate><volume>20</volume><issue>11</issue><spage>2174</spage><epage>2181</epage><pages>2174-2181</pages><issn>1044-0305</issn><eissn>1879-1123</eissn><abstract>We investigated the influence of peptide size on the apparent loss of sequence during collision-induced dissociation (CID) of
b ions using a group of peptides containing from between 4 and 10 residues. Although scrambling of sequence for
b
3
+ generated from tetrapeptides is minimal, significant formation of nondirect sequence ions (i.e., ions for which scrambling has apparently occurred) was observed for all larger
b ions included in the study.
Multiple-stage CID experiments demonstrate loss of internal residues and remarkable similarity of product ion spectra among
b
n
ions from permuted sequence isomers. The results support the hypothesis that significant sequence scrambling can occur following fragmentation of
b-type ions.</abstract><cop>New York</cop><pub>Elsevier Inc</pub><pmid>19758821</pmid><doi>10.1016/j.jasms.2009.07.023</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; SpringerLink Journals - AutoHoldings |
| subjects | Amino Acid Sequence Analytical Chemistry Analytical, structural and metabolic biochemistry Base Sequence Bioinformatics Biological and medical sciences Biotechnology Chemistry Chemistry and Materials Science Fundamental and applied biological sciences. Psychology General aspects, investigation methods Ions - classification Isomerism Mass spectrometry Molecular Sequence Data Molecular Structure Oligopeptides - chemical synthesis Oligopeptides - chemistry Organic Chemistry Peptides Proteins Proteomics Residues Spectrometry, Mass, Electrospray Ionization |
| title | Influence of Size on Apparent Scrambling of Sequence During CID of b-Type Ions |
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