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Electron-transfer dissociation

January 01, 1970

Electron-transfer dissociation (ETD) is a method of fragmenting multiply-charged gaseous macromolecules in a mass spectrometer between the stages of tandem mass spectrometry (MS/MS).[1] Similar to electron-capture dissociation, ETD induces fragmentation of large, multiply-charged cations by transferring electrons to them.[2] ETD is used extensively with polymers and biological molecules such as proteins and peptides for sequence analysis.[3] Transferring an electron causes peptide backbone cleavage into c- and z-ions while leaving labile post translational modifications (PTM) intact.[4] The technique only works well for higher charge state peptide or polymer ions (z>2).[2] However, relative to collision-induced dissociation (CID), ETD is advantageous for the fragmentation of longer peptides or even entire proteins.[5] This makes the technique important for top-down proteomics. The method was developed by Hunt and coworkers at the University of Virginia.[6]

An ion trap mass spectrometer with electron transfer dissociation capability
Peptide fragmentation notation

History edit

Electron-capture dissociation (ECD) was developed in 1998 to fragment large proteins for mass spectrometric analysis.[7] Because ECD requires a large amount of near-thermal electrons (<0.2eV), originally it was used exclusively with Fourier transform ion cyclotron resonance mass spectrometry (FTICR), the most expensive form of MS instrumentation.[8] Less costly options such as quadrupole time-of-flight (Q-TOF), quadrupole ion trap (QIT) and linear quadrupole ion trap (QLT) instruments used the more energy-intensive collision-induced dissociation method (CID), resulting in random fragmentation of peptides and proteins.[9] In 2004 Syka et al. announced the creation of ETD, a dissociation method similar to ECD, but using a low-cost, widely available commercial spectrometer. The first ETD experiments were run on a QLT mass spectrometer with an electrospray ionization (ESI) source.[10]

Principle of operation edit

Several steps are involved in electron transfer dissociation. Usually a protein mixture is first separated using high performance liquid chromatography (HPLC). Next multiply-protonated precursor molecules are generated by electrospray ionization and injected into the mass spectrometer. (Only molecules with a charge of 2+ or greater can be used in ETD.) In order for an electron to be transferred to the positive precursor molecules radical anions are generated and put into the ion trap with them. During the ion/ion reaction an electron is transferred to the positively-charged protein or peptide, causing fragmentation along the peptide backbone. Finally the resultant fragments are mass analyzed.[11]

Radical anion preparation edit

In the original ETD experiments anthracene (C14H10) was used to generate reactive radical anions through negative chemical ionization.[10] Several polycyclic aromatic hydrocarbon molecules have been used in subsequent experiments, with fluoranthene currently the preferred reagent.[12] Fluoranthene has only about 40% efficiency in electron transfer, however, so other molecules with low electron affinity are being sought.[11]

Injection and fragmentation edit

 
Multiply-charged precursor ion reacts with radical anion

When the precursor cations (proteins or peptides) and radical anions are combined in the ion trap an electron is transferred to the multiply-charged cation. This forms an unstable positive radical cation with one less positive charge and an odd electron.[13] Fragmentation takes place along the peptide backbone at a N− Cα bond, resulting in c- and z-type fragment ions.[14]

 
Protein or peptide radical cation fragments into c-ion and z-ion

Mass analysis edit

Fragmentation caused by ETD allows more complete protein sequence information to be obtained from ETD spectra than from CID tandem mass spectrometry. Because many peptide backbone c- and z- type ions are detected, almost complete sequence coverage of many peptides can be discerned from ETD fragmentation spectra.[15] Sequences of 15-40 amino acids at both the N-terminus and the C-terminus of the protein can be read using mass-to-charge values for the singly and doubly charged ions. These sequences, together with the measured mass of the intact protein, can be compared to database entries for known proteins and to reveal post-translational modifications.[16]

Instrumentation edit

 
Schematic diagram of LTQ with ETD
 
Bruker high capacity ion trap with ETD (schematic diagram) 

Electron transfer dissociation takes place in an ion trap mass spectrometer with an electrospray ionization source. The first ETD experiments at the University of Virginia utilized a radio frequency quadrupole linear ion trap (LQT) modified with a chemical ionization (CI) source at the back side of the instrument (see diagram at right).[10] Because a spectrum can be obtained in about 300 milliseconds, liquid chromatography is often coupled with the ETD MS/MS.[11] The disadvantage of using LQT is that the mass resolving power is less than that of other mass spectrometers.[14]

Subsequent studies have tried other instrumentation to improve mass resolution. Having a negative CI source at the back of the instrument interfered with the high-resolution analyzer in LQT-Orbitrap and quadrupole time-of-flight (QTOF), so alternate ionization methods for the radical anions have been introduced.[11]

In 2006 a group at Purdue University led by Scott McLuckey used a quadrupole/time-of-flight (QqTOF) tandem mass spectrometer with pulsed nano-ESI/atmospheric pressure chemical ionization (APCI) dual ionization source using radical anions of 1,3-dinitrobenzene as the electron donor.[17] Later a lab at the University of Wisconsin adapted a hybrid quadrupole linear ion trap-orbitrap mass spectrometer to use ETD. This method also used a front-end ionization method for the radical anions of 9-anthracenecarboxylic acid via pulsed dual ESI sources.[18]

As ETD is increasingly popular for protein and peptide structure analysis, implementation on easily available ion-trap mass spectrometers coupled with high resolution mass analyzers continues to evolve.[19]

Applications edit

Proteomics edit

ETD is widely used in the analysis of protein and large peptides. Important post translational modifications including phosphorylation, glycosylation and disulfide linkages are all analyzed using ETD.[20]

Polymer chemistry edit

Although MS-based analyses of polymers have largely been performed using single-stage MS, tandem MS has also been used to characterize polymer components. CID is the most common method of dissociation used, but ETD has been used as a complementary method. Unique bond cleavages resulting from ETD supply valuable diagnostic information.[2]

See also edit

References edit

  1. ^ Dass, Chhabil (2007). Fundamentals of Contemporary Mass Spectrometry. Hoboken, New Jersey: John Wiley & Sons. p. 128. ISBN 978-0-470-11848-1.
  2. ^ a b c Hart-Smith, Gene (2014-01-15). "A review of electron-capture and electron-transfer dissociation tandem mass spectrometry in polymer chemistry". Analytica Chimica Acta. Polymer Mass Spectrometry. 808: 44–55. doi:10.1016/j.aca.2013.09.033. PMID 24370092.
  3. ^ Brodbelt, Jennifer S. (2015-12-11). "Ion Activation Methods for Peptides and Proteins". Analytical Chemistry. 88 (1): 30–51. doi:10.1021/acs.analchem.5b04563. PMC 5553572. PMID 26630359.
  4. ^ Coon, Joshua J.; Syka, John E.P.; Shabanowitz, Jeffrey; Hunt, Donald F. (April 2005). . BioTechniques. 38 (4): 519, 521, 523. doi:10.2144/05384te01. PMID 15884666. Archived from the original on May 13, 2016. Retrieved April 15, 2016.
  5. ^ Good, David M.; Wirtala, Matthew; McAlister, Graeme C.; Coon, Joshua J. (2007-11-01). "Performance Characteristics of Electron Transfer Dissociation Mass Spectrometry". Molecular & Cellular Proteomics. 6 (11): 1942–1951. doi:10.1074/mcp.M700073-MCP200. ISSN 1535-9476. PMID 17673454.
  6. ^ US patent 7534622, Donald F. Hunt, Joshua J. Coon, John E.P. Syka, Jarrod A. Marto, "Electron transfer dissociation for biopolymer sequence mass spectrometric analysis", issued 2009-05-19 
  7. ^ Zubarev, Roman A.; Kelleher, Neil L.; McLafferty, Fred W. (1998-04-01). "Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process". Journal of the American Chemical Society. 120 (13): 3265–3266. doi:10.1021/ja973478k. ISSN 0002-7863.
  8. ^ McLafferty, Fred W.; Horn, David M.; Breuker, Kathrin; Ge, Ying; Lewis, Mark A.; Cerda, Blas; Zubarev, Roman A.; Carpenter, Barry K. (2001-03-01). "Electron capture dissociation of gaseous multiply charged ions by Fourier-transform ion cyclotron resonance". Journal of the American Society for Mass Spectrometry. 12 (3): 245–249. doi:10.1016/S1044-0305(00)00223-3. ISSN 1044-0305. PMID 11281599. S2CID 45275450.
  9. ^ Mitchell Wells, J.; McLuckey, Scott A. (2005-01-01). "Collision‐Induced Dissociation (CID) of Peptides and Proteins". Biological Mass Spectrometry. Methods in Enzymology. Vol. 402. pp. 148–185. doi:10.1016/s0076-6879(05)02005-7. ISBN 9780121828073. PMID 16401509.
  10. ^ a b c Syka JE, Coon JJ, Schroeder MJ, Shabanowitz J, Hunt DF (2004). "Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry". Proc. Natl. Acad. Sci. U.S.A. 101 (26): 9528–33. Bibcode:2004PNAS..101.9528S. doi:10.1073/pnas.0402700101. PMC 470779. PMID 15210983.
  11. ^ a b c d Kim, Min-Sik; Pandey, Akhilesh (2012-02-01). "Electron transfer dissociation mass spectrometry in proteomics". Proteomics. 12 (4–5): 530–542. doi:10.1002/pmic.201100517. ISSN 1615-9861. PMC 3664229. PMID 22246976.
  12. ^ Chi, An; Huttenhower, Curtis; Geer, Lewis Y.; Coon, Joshua J.; Syka, John E. P.; Bai, Dina L.; Shabanowitz, Jeffrey; Burke, Daniel J.; Troyanskaya, Olga G. (2007-02-13). "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry". Proceedings of the National Academy of Sciences. 104 (7): 2193–2198. Bibcode:2007PNAS..104.2193C. doi:10.1073/pnas.0607084104. ISSN 0027-8424. PMC 1892997. PMID 17287358.
  13. ^ "Electron Transfer Dissociation". The National High Magnetic Field Laboratory. August 28, 2015. Retrieved March 1, 2016.
  14. ^ a b Qi, Yulin; Volmer, Dietrich A. (2015-10-01). "Electron-based fragmentation methods in mass spectrometry: An overview". Mass Spectrometry Reviews. 36 (1): 4–15. Bibcode:2017MSRv...36....4Q. doi:10.1002/mas.21482. ISSN 1098-2787. PMID 26445267.
  15. ^ Zhang, Qibin; Frolov, Andrej; Tang, Ning; Hoffmann, Ralf; van de Goor, Tom; Metz, Thomas O.; Smith, Richard D. (2007-03-15). "Application of electron transfer dissociation mass spectrometry in analyses of non-enzymatically glycated peptides". Rapid Communications in Mass Spectrometry. 21 (5): 661–666. Bibcode:2007RCMS...21..661Z. doi:10.1002/rcm.2884. ISSN 1097-0231. PMC 2731431. PMID 17279487.
  16. ^ Chi, An; Bai, Dina L.; Geer, Lewis Y.; Shabanowitz, Jeffrey; Hunt, Donald F. (2007-01-01). "Analysis of intact proteins on a chromatographic time scale by electron transfer dissociation tandem mass spectrometry". International Journal of Mass Spectrometry. Donald F. Hunt Honour Issue. 259 (1–3): 197–203. Bibcode:2007IJMSp.259..197C. doi:10.1016/j.ijms.2006.09.030. PMC 1826913. PMID 17364019.
  17. ^ Xia, Yu; Chrisman, Paul A.; Erickson, David E.; Liu, Jian; Liang, Xiaorong; Londry, Frank A.; Yang, Min J.; McLuckey, Scott A. (2006-06-01). "Implementation of Ion/Ion Reactions in a Quadrupole/Time-of-Flight Tandem Mass Spectrometer". Analytical Chemistry. 78 (12): 4146–4154. doi:10.1021/ac0606296. ISSN 0003-2700. PMC 2575740. PMID 16771545.
  18. ^ McAlister, Graeme C.; Phanstiel, Doug; Good, David M.; Berggren, W. Travis; Coon, Joshua J. (2007-05-01). "Implementation of Electron-Transfer Dissociation on a Hybrid Linear Ion Trap−Orbitrap Mass Spectrometer". Analytical Chemistry. 79 (10): 3525–3534. doi:10.1021/ac070020k. ISSN 0003-2700. PMC 2662514. PMID 17441688.
  19. ^ Zhurov, Konstantin O.; Fornelli, Luca; Wodrich, Matthew D.; Laskay, Ünige A.; Tsybin, Yury O. (2013-05-28). "Principles of electron capture and transfer dissociation mass spectrometry applied to peptide and protein structure analysis". Chemical Society Reviews. 42 (12): 5014–30. doi:10.1039/c3cs35477f. ISSN 1460-4744. PMID 23450212.
  20. ^ Wiesner, Julia; Premsler, Thomas; Sickmann, Albert (2008-11-01). "Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications". Proteomics. 8 (21): 4466–4483. doi:10.1002/pmic.200800329. ISSN 1615-9861. PMID 18972526. S2CID 206362597.

January 01, 1970
electron, transfer, dissociation, method, fragmenting, multiply, charged, gaseous, macromolecules, mass, spectrometer, between, stages, tandem, mass, spectrometry, similar, electron, capture, dissociation, induces, fragmentation, large, multiply, charged, cati. Electron transfer dissociation ETD is a method of fragmenting multiply charged gaseous macromolecules in a mass spectrometer between the stages of tandem mass spectrometry MS MS 1 Similar to electron capture dissociation ETD induces fragmentation of large multiply charged cations by transferring electrons to them 2 ETD is used extensively with polymers and biological molecules such as proteins and peptides for sequence analysis 3 Transferring an electron causes peptide backbone cleavage into c and z ions while leaving labile post translational modifications PTM intact 4 The technique only works well for higher charge state peptide or polymer ions z gt 2 2 However relative to collision induced dissociation CID ETD is advantageous for the fragmentation of longer peptides or even entire proteins 5 This makes the technique important for top down proteomics The method was developed by Hunt and coworkers at the University of Virginia 6 An ion trap mass spectrometer with electron transfer dissociation capability Peptide fragmentation notation Contents 1 History 2 Principle of operation 2 1 Radical anion preparation 2 2 Injection and fragmentation 2 3 Mass analysis 3 Instrumentation 4 Applications 4 1 Proteomics 4 2 Polymer chemistry 5 See also 6 ReferencesHistory editElectron capture dissociation ECD was developed in 1998 to fragment large proteins for mass spectrometric analysis 7 Because ECD requires a large amount of near thermal electrons lt 0 2eV originally it was used exclusively with Fourier transform ion cyclotron resonance mass spectrometry FTICR the most expensive form of MS instrumentation 8 Less costly options such as quadrupole time of flight Q TOF quadrupole ion trap QIT and linear quadrupole ion trap QLT instruments used the more energy intensive collision induced dissociation method CID resulting in random fragmentation of peptides and proteins 9 In 2004 Syka et al announced the creation of ETD a dissociation method similar to ECD but using a low cost widely available commercial spectrometer The first ETD experiments were run on a QLT mass spectrometer with an electrospray ionization ESI source 10 Principle of operation editSeveral steps are involved in electron transfer dissociation Usually a protein mixture is first separated using high performance liquid chromatography HPLC Next multiply protonated precursor molecules are generated by electrospray ionization and injected into the mass spectrometer Only molecules with a charge of 2 or greater can be used in ETD In order for an electron to be transferred to the positive precursor molecules radical anions are generated and put into the ion trap with them During the ion ion reaction an electron is transferred to the positively charged protein or peptide causing fragmentation along the peptide backbone Finally the resultant fragments are mass analyzed 11 Radical anion preparation edit In the original ETD experiments anthracene C14H10 was used to generate reactive radical anions through negative chemical ionization 10 Several polycyclic aromatic hydrocarbon molecules have been used in subsequent experiments with fluoranthene currently the preferred reagent 12 Fluoranthene has only about 40 efficiency in electron transfer however so other molecules with low electron affinity are being sought 11 Injection and fragmentation edit nbsp Multiply charged precursor ion reacts with radical anion When the precursor cations proteins or peptides and radical anions are combined in the ion trap an electron is transferred to the multiply charged cation This forms an unstable positive radical cation with one less positive charge and an odd electron 13 Fragmentation takes place along the peptide backbone at a N Ca bond resulting in c and z type fragment ions 14 nbsp Protein or peptide radical cation fragments into c ion and z ion Mass analysis edit Fragmentation caused by ETD allows more complete protein sequence information to be obtained from ETD spectra than from CID tandem mass spectrometry Because many peptide backbone c and z type ions are detected almost complete sequence coverage of many peptides can be discerned from ETD fragmentation spectra 15 Sequences of 15 40 amino acids at both the N terminus and the C terminus of the protein can be read using mass to charge values for the singly and doubly charged ions These sequences together with the measured mass of the intact protein can be compared to database entries for known proteins and to reveal post translational modifications 16 Instrumentation edit nbsp Schematic diagram of LTQ with ETD nbsp Bruker high capacity ion trap with ETD schematic diagram Electron transfer dissociation takes place in an ion trap mass spectrometer with an electrospray ionization source The first ETD experiments at the University of Virginia utilized a radio frequency quadrupole linear ion trap LQT modified with a chemical ionization CI source at the back side of the instrument see diagram at right 10 Because a spectrum can be obtained in about 300 milliseconds liquid chromatography is often coupled with the ETD MS MS 11 The disadvantage of using LQT is that the mass resolving power is less than that of other mass spectrometers 14 Subsequent studies have tried other instrumentation to improve mass resolution Having a negative CI source at the back of the instrument interfered with the high resolution analyzer in LQT Orbitrap and quadrupole time of flight QTOF so alternate ionization methods for the radical anions have been introduced 11 In 2006 a group at Purdue University led by Scott McLuckey used a quadrupole time of flight QqTOF tandem mass spectrometer with pulsed nano ESI atmospheric pressure chemical ionization APCI dual ionization source using radical anions of 1 3 dinitrobenzene as the electron donor 17 Later a lab at the University of Wisconsin adapted a hybrid quadrupole linear ion trap orbitrap mass spectrometer to use ETD This method also used a front end ionization method for the radical anions of 9 anthracenecarboxylic acid via pulsed dual ESI sources 18 As ETD is increasingly popular for protein and peptide structure analysis implementation on easily available ion trap mass spectrometers coupled with high resolution mass analyzers continues to evolve 19 Applications editProteomics edit ETD is widely used in the analysis of protein and large peptides Important post translational modifications including phosphorylation glycosylation and disulfide linkages are all analyzed using ETD 20 Polymer chemistry edit Although MS based analyses of polymers have largely been performed using single stage MS tandem MS has also been used to characterize polymer components CID is the most common method of dissociation used but ETD has been used as a complementary method Unique bond cleavages resulting from ETD supply valuable diagnostic information 2 See also editNegative electron transfer dissociation Tandem mass spectrometry ElectrosprayReferences edit Dass Chhabil 2007 Fundamentals of Contemporary Mass Spectrometry Hoboken New Jersey John Wiley amp Sons p 128 ISBN 978 0 470 11848 1 a b c Hart Smith Gene 2014 01 15 A review of electron capture and electron transfer dissociation tandem mass spectrometry in polymer chemistry Analytica Chimica Acta Polymer Mass Spectrometry 808 44 55 doi 10 1016 j aca 2013 09 033 PMID 24370092 Brodbelt Jennifer S 2015 12 11 Ion Activation Methods for Peptides and Proteins Analytical Chemistry 88 1 30 51 doi 10 1021 acs analchem 5b04563 PMC 5553572 PMID 26630359 Coon Joshua J Syka John E P Shabanowitz Jeffrey Hunt Donald F April 2005 Tandem Mass Spectrometry for Peptide and Protein Sequence Analysis BioTechniques 38 4 519 521 523 doi 10 2144 05384te01 PMID 15884666 Archived from the original on May 13 2016 Retrieved April 15 2016 Good David M Wirtala Matthew McAlister Graeme C Coon Joshua J 2007 11 01 Performance Characteristics of Electron Transfer Dissociation Mass Spectrometry Molecular amp Cellular Proteomics 6 11 1942 1951 doi 10 1074 mcp M700073 MCP200 ISSN 1535 9476 PMID 17673454 US patent 7534622 Donald F Hunt Joshua J Coon John E P Syka Jarrod A Marto Electron transfer dissociation for biopolymer sequence mass spectrometric analysis issued 2009 05 19 Zubarev Roman A Kelleher Neil L McLafferty Fred W 1998 04 01 Electron Capture Dissociation of Multiply Charged Protein Cations A Nonergodic Process Journal of the American Chemical Society 120 13 3265 3266 doi 10 1021 ja973478k ISSN 0002 7863 McLafferty Fred W Horn David M Breuker Kathrin Ge Ying Lewis Mark A Cerda Blas Zubarev Roman A Carpenter Barry K 2001 03 01 Electron capture dissociation of gaseous multiply charged ions by Fourier transform ion cyclotron resonance Journal of the American Society for Mass Spectrometry 12 3 245 249 doi 10 1016 S1044 0305 00 00223 3 ISSN 1044 0305 PMID 11281599 S2CID 45275450 Mitchell Wells J McLuckey Scott A 2005 01 01 Collision Induced Dissociation CID of Peptides and Proteins Biological Mass Spectrometry Methods in Enzymology Vol 402 pp 148 185 doi 10 1016 s0076 6879 05 02005 7 ISBN 9780121828073 PMID 16401509 a b c Syka JE Coon JJ Schroeder MJ Shabanowitz J Hunt DF 2004 Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry Proc Natl Acad Sci U S A 101 26 9528 33 Bibcode 2004PNAS 101 9528S doi 10 1073 pnas 0402700101 PMC 470779 PMID 15210983 a b c d Kim Min Sik Pandey Akhilesh 2012 02 01 Electron transfer dissociation mass spectrometry in proteomics Proteomics 12 4 5 530 542 doi 10 1002 pmic 201100517 ISSN 1615 9861 PMC 3664229 PMID 22246976 Chi An Huttenhower Curtis Geer Lewis Y Coon Joshua J Syka John E P Bai Dina L Shabanowitz Jeffrey Burke Daniel J Troyanskaya Olga G 2007 02 13 Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation ETD mass spectrometry Proceedings of the National Academy of Sciences 104 7 2193 2198 Bibcode 2007PNAS 104 2193C doi 10 1073 pnas 0607084104 ISSN 0027 8424 PMC 1892997 PMID 17287358 Electron Transfer Dissociation The National High Magnetic Field Laboratory August 28 2015 Retrieved March 1 2016 a b Qi Yulin Volmer Dietrich A 2015 10 01 Electron based fragmentation methods in mass spectrometry An overview Mass Spectrometry Reviews 36 1 4 15 Bibcode 2017MSRv 36 4Q doi 10 1002 mas 21482 ISSN 1098 2787 PMID 26445267 Zhang Qibin Frolov Andrej Tang Ning Hoffmann Ralf van de Goor Tom Metz Thomas O Smith Richard D 2007 03 15 Application of electron transfer dissociation mass spectrometry in analyses of non enzymatically glycated peptides Rapid Communications in Mass Spectrometry 21 5 661 666 Bibcode 2007RCMS 21 661Z doi 10 1002 rcm 2884 ISSN 1097 0231 PMC 2731431 PMID 17279487 Chi An Bai Dina L Geer Lewis Y Shabanowitz Jeffrey Hunt Donald F 2007 01 01 Analysis of intact proteins on a chromatographic time scale by electron transfer dissociation tandem mass spectrometry International Journal of Mass Spectrometry Donald F Hunt Honour Issue 259 1 3 197 203 Bibcode 2007IJMSp 259 197C doi 10 1016 j ijms 2006 09 030 PMC 1826913 PMID 17364019 Xia Yu Chrisman Paul A Erickson David E Liu Jian Liang Xiaorong Londry Frank A Yang Min J McLuckey Scott A 2006 06 01 Implementation of Ion Ion Reactions in a Quadrupole Time of Flight Tandem Mass Spectrometer Analytical Chemistry 78 12 4146 4154 doi 10 1021 ac0606296 ISSN 0003 2700 PMC 2575740 PMID 16771545 McAlister Graeme C Phanstiel Doug Good David M Berggren W Travis Coon Joshua J 2007 05 01 Implementation of Electron Transfer Dissociation on a Hybrid Linear Ion Trap Orbitrap Mass Spectrometer Analytical Chemistry 79 10 3525 3534 doi 10 1021 ac070020k ISSN 0003 2700 PMC 2662514 PMID 17441688 Zhurov Konstantin O Fornelli Luca Wodrich Matthew D Laskay Unige A Tsybin Yury O 2013 05 28 Principles of electron capture and transfer dissociation mass spectrometry applied to peptide and protein structure analysis Chemical Society Reviews 42 12 5014 30 doi 10 1039 c3cs35477f ISSN 1460 4744 PMID 23450212 Wiesner Julia Premsler Thomas Sickmann Albert 2008 11 01 Application of electron transfer dissociation ETD for the analysis of posttranslational modifications Proteomics 8 21 4466 4483 doi 10 1002 pmic 200800329 ISSN 1615 9861 PMID 18972526 S2CID 206362597 Retrieved from https en wikipedia org w index php title Electron transfer dissociation amp oldid 1211393253, wikipedia, wiki, book, books, library,

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