Electron Transfer Dissociation Reveals Changes in the Cleavage Frequencies of Backbone Bonds Distant to Amide-to-Ester Substitutions in Polypeptides
Interrogation of electron transfer dissociation (ETD) mass spectra of peptide amide-to-ester backbone bond substituted analogues (depsipeptides) reveals substantial differences in the entire backbone cleavage frequencies. It is suggested that the point permutation of backbone bonds leads to changes...
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| Veröffentlicht in: | Journal of the American Society for Mass Spectrometry 2011-11, Vol.22 (11), p.1953-1957, Article s13361-011-0242-5 |
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| container_end_page | 1957 |
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| container_issue | 11 |
| container_start_page | 1953 |
| container_title | Journal of the American Society for Mass Spectrometry |
| container_volume | 22 |
| creator | Hansen, Thomas A. Jung, Hye R. Kjeldsen, Frank |
| description | Interrogation of electron transfer dissociation (ETD) mass spectra of peptide amide-to-ester backbone bond substituted analogues (depsipeptides) reveals substantial differences in the entire backbone cleavage frequencies. It is suggested that the point permutation of backbone bonds leads to changes in the predominant ion structures by removal/weakening of specific hydrogen bonding. ETD responds to these changes by redistributing the cleavage frequencies of the peptide backbone bonds. In comparison, no distinction between depsi-/peptide was observed using collision-activated dissociation, which is consistent with a general unfolding and elimination of structural information of these ions. These results should encourage further exploration of depsipeptides for gas-phase structural characterization. |
| doi_str_mv | 10.1007/s13361-011-0242-5 |
| format | Article |
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It is suggested that the point permutation of backbone bonds leads to changes in the predominant ion structures by removal/weakening of specific hydrogen bonding. ETD responds to these changes by redistributing the cleavage frequencies of the peptide backbone bonds. In comparison, no distinction between depsi-/peptide was observed using collision-activated dissociation, which is consistent with a general unfolding and elimination of structural information of these ions. These results should encourage further exploration of depsipeptides for gas-phase structural characterization.</description><identifier>ISSN: 1044-0305</identifier><identifier>EISSN: 1879-1123</identifier><identifier>DOI: 10.1007/s13361-011-0242-5</identifier><identifier>PMID: 21952783</identifier><language>eng</language><publisher>New York: Springer-Verlag</publisher><subject>Amides - chemistry ; Amino Acid Sequence ; Aminoacids, peptides. Hormones. Neuropeptides ; Analytical Chemistry ; Analytical, structural and metabolic biochemistry ; Backbone ; Bioinformatics ; Biological and medical sciences ; Biotechnology ; Bonding strength ; Chemical bonds ; Chemistry ; Chemistry and Materials Science ; Cleavage ; Depsipeptides - chemistry ; Electron transfer ; Electrons ; Fundamental and applied biological sciences. Psychology ; Hydrogen Bonding ; Interrogation ; Ions ; Mass spectra ; Mass spectrometry ; Mass Spectrometry - methods ; Molecular Sequence Data ; Organic Chemistry ; Peptides ; Peptides - chemistry ; Polypeptides ; Proteins ; Proteomics ; Research Article ; Structural analysis</subject><ispartof>Journal of the American Society for Mass Spectrometry, 2011-11, Vol.22 (11), p.1953-1957, Article s13361-011-0242-5</ispartof><rights>American Society for Mass Spectrometry 2011</rights><rights>2015 INIST-CNRS</rights><rights>Journal of The American Society for Mass Spectrometry is a copyright of Springer, 2011.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c444t-4637100a801b78506ac5116b4a90d1c422d6f05c702a9ce0e08013b74f6463493</citedby><cites>FETCH-LOGICAL-c444t-4637100a801b78506ac5116b4a90d1c422d6f05c702a9ce0e08013b74f6463493</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s13361-011-0242-5$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s13361-011-0242-5$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25448007$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21952783$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hansen, Thomas A.</creatorcontrib><creatorcontrib>Jung, Hye R.</creatorcontrib><creatorcontrib>Kjeldsen, Frank</creatorcontrib><title>Electron Transfer Dissociation Reveals Changes in the Cleavage Frequencies of Backbone Bonds Distant to Amide-to-Ester Substitutions in Polypeptides</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>Interrogation of electron transfer dissociation (ETD) mass spectra of peptide amide-to-ester backbone bond substituted analogues (depsipeptides) reveals substantial differences in the entire backbone cleavage frequencies. It is suggested that the point permutation of backbone bonds leads to changes in the predominant ion structures by removal/weakening of specific hydrogen bonding. ETD responds to these changes by redistributing the cleavage frequencies of the peptide backbone bonds. In comparison, no distinction between depsi-/peptide was observed using collision-activated dissociation, which is consistent with a general unfolding and elimination of structural information of these ions. These results should encourage further exploration of depsipeptides for gas-phase structural characterization.</description><subject>Amides - chemistry</subject><subject>Amino Acid Sequence</subject><subject>Aminoacids, peptides. Hormones. Neuropeptides</subject><subject>Analytical Chemistry</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Backbone</subject><subject>Bioinformatics</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Bonding strength</subject><subject>Chemical bonds</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Cleavage</subject><subject>Depsipeptides - chemistry</subject><subject>Electron transfer</subject><subject>Electrons</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen Bonding</subject><subject>Interrogation</subject><subject>Ions</subject><subject>Mass spectra</subject><subject>Mass spectrometry</subject><subject>Mass Spectrometry - methods</subject><subject>Molecular Sequence Data</subject><subject>Organic Chemistry</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Polypeptides</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Research Article</subject><subject>Structural analysis</subject><issn>1044-0305</issn><issn>1879-1123</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp1kd1u1DAQhSMEoqXwANwgSwhxFbBjO04u22ULSJVAUK4tx5m0Lll78TiV-h48MLPs8iMkLixbnm_OGftU1VPBXwnOzWsUUrai5oJWo5pa36uORWf6WohG3qczV6rmkuuj6hHiDefC8N48rI4a0evGdPK4-r6ewZecIrvMLuIEmb0JiMkHVwLdfoJbcDOy1bWLV4AsRFauga1mcLfuCth5hm8LRB-oliZ25vzXIUVgZymOuJMqLhZWEjvdhBHqkuo1FjL5vAxYQll2Jj9VP6b5bgvbQhQ-rh5MZApPDvtJ9eV8fbl6V198ePt-dXpRe6VUqVUrDf2D67gYTKd567wWoh2U6_kovGqasZ249oY3rvfAgRMpB6OmllpVL0-ql3vdbU70Cix2E9DDPLsIaUHb9aSqeymIfP4PeZOWHGk4S18puNZCKqLEnvI5IWaY7DaHjct3VnC7S8zuE7OUmN0lZjX1PDsoL8MGxt8dvyIi4MUBcOjdPFFMPuAfTivVkTRxzZ5DKlFW-a8R_-v-A3D0rZ4</recordid><startdate>20111101</startdate><enddate>20111101</enddate><creator>Hansen, Thomas A.</creator><creator>Jung, Hye R.</creator><creator>Kjeldsen, Frank</creator><general>Springer-Verlag</general><general>Elsevier</general><general>Springer Nature B.V</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>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>7X8</scope></search><sort><creationdate>20111101</creationdate><title>Electron Transfer Dissociation Reveals Changes in the Cleavage Frequencies of Backbone Bonds Distant to Amide-to-Ester Substitutions in Polypeptides</title><author>Hansen, Thomas A. ; Jung, Hye R. ; Kjeldsen, Frank</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c444t-4637100a801b78506ac5116b4a90d1c422d6f05c702a9ce0e08013b74f6463493</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amides - chemistry</topic><topic>Amino Acid Sequence</topic><topic>Aminoacids, peptides. Hormones. Neuropeptides</topic><topic>Analytical Chemistry</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Backbone</topic><topic>Bioinformatics</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Bonding strength</topic><topic>Chemical bonds</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Cleavage</topic><topic>Depsipeptides - chemistry</topic><topic>Electron transfer</topic><topic>Electrons</topic><topic>Fundamental and applied biological sciences. 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Am. Soc. Mass Spectrom</stitle><addtitle>J Am Soc Mass Spectrom</addtitle><date>2011-11-01</date><risdate>2011</risdate><volume>22</volume><issue>11</issue><spage>1953</spage><epage>1957</epage><pages>1953-1957</pages><artnum>s13361-011-0242-5</artnum><issn>1044-0305</issn><eissn>1879-1123</eissn><abstract>Interrogation of electron transfer dissociation (ETD) mass spectra of peptide amide-to-ester backbone bond substituted analogues (depsipeptides) reveals substantial differences in the entire backbone cleavage frequencies. It is suggested that the point permutation of backbone bonds leads to changes in the predominant ion structures by removal/weakening of specific hydrogen bonding. ETD responds to these changes by redistributing the cleavage frequencies of the peptide backbone bonds. 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| identifier | ISSN: 1044-0305 |
| ispartof | Journal of the American Society for Mass Spectrometry, 2011-11, Vol.22 (11), p.1953-1957, Article s13361-011-0242-5 |
| issn | 1044-0305 1879-1123 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_898505931 |
| source | MEDLINE; SpringerNature Journals |
| subjects | Amides - chemistry Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical Chemistry Analytical, structural and metabolic biochemistry Backbone Bioinformatics Biological and medical sciences Biotechnology Bonding strength Chemical bonds Chemistry Chemistry and Materials Science Cleavage Depsipeptides - chemistry Electron transfer Electrons Fundamental and applied biological sciences. Psychology Hydrogen Bonding Interrogation Ions Mass spectra Mass spectrometry Mass Spectrometry - methods Molecular Sequence Data Organic Chemistry Peptides Peptides - chemistry Polypeptides Proteins Proteomics Research Article Structural analysis |
| title | Electron Transfer Dissociation Reveals Changes in the Cleavage Frequencies of Backbone Bonds Distant to Amide-to-Ester Substitutions in Polypeptides |
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