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Electron Capture Dissociation Fourier Transform Ion Cyclotron Resonance Mass Spectrometry in the Electron Energy Range 0-50 eV
Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Ion Physics.
2004 (English)In: Rapid Communications in Mass Spectrometry, ISSN 0951-4198, E-ISSN 1097-0231, Vol. 18, no 14, 1607-1613 p.Article in journal (Refereed) Published
Abstract [en]

Electron capture dissociation (ECD) of polypeptide cations was obtained with pencil and hollow electron beams for both sidekick and gas-assisted dynamic ion trapping (GADT) using Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) with an electrostatic ion transfer line. Increasing the number of trapped ions by multiple ICR trap loads using GADT improved the ECD sensitivity in comparison with sidekick ion trapping and ECD efficiency in comparison with single ion trap load by GADT. Furthermore, enhanced sensitivity made it possible to observe ECD in a wide range of electron energies (0-50 eV). The degree, rate and fragmentation characteristics of ECD FTICR-MS were investigated as functions of electron energy, electron irradiation time, electron flux and ion trapping parameters for this broad energy range. The results obtained show that the rate of ECD is higher for more energetic (>1 eV) electrons. Long electron irradiation time with energetic electrons reduces average fragment ion mass and decreases efficiency of formation of c- and z-type ions. The obtained dependencies suggest that the average fragment ion mass and the ECD efficiency are functions of the total fluence of the electron beam (electron energy multiplied by irradiation time). The measured electron energy distributions in low-energy ECD and hot ECD regimes are about 1 eV at full width half maximum in employed experimental configurations.

Place, publisher, year, edition, pages
2004. Vol. 18, no 14, 1607-1613 p.
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:uu:diva-91524DOI: 10.1002/rcm.1525PubMedID: 15282786OAI: oai:DiVA.org:uu-91524DiVA: diva2:164287
Available from: 2004-03-25 Created: 2004-03-25 Last updated: 2017-12-14Bibliographically approved
In thesis
1. High Rate Electron Capture Dissociation Fourier Transform Ion Cyclotron Resonance Mass Spectrometry
Open this publication in new window or tab >>High Rate Electron Capture Dissociation Fourier Transform Ion Cyclotron Resonance Mass Spectrometry
2004 (English)Doctoral thesis, comprehensive summary (Other academic)
Alternative title[sv]
Snabb fragmenteringsmetod genom elektroninfågning i Fouriertransform-joncyklotronresonans-masspektrometri
Abstract [en]

Advances in science and technology during the past decade have greatly enhanced the level of the structural investigation of macromolecules – peptides and proteins. Biological mass spectrometry has become one of the most precise and sensitive techniques in peptide and protein analysis. However, increasing demands of biotechnological applications require further progress to be made.

In the present thesis the development and improvement of peptide and protein characterization methods and techniques based on ion-electron and ion-photon reactions in electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry are described. The focus is on the development of the electron capture dissociation method, recently discovered by the group of professor McLafferty, into a high rate, efficient tandem mass spectrometrical technique.

The rate and reliability of the electron capture dissociation technique were greatly increased by implementation of low-energy pencil electron beam injection systems based on indirectly heated dispenser cathodes. Further implementation of a hollow electron beam injection system combined, in a single experimental configuration, two rapid fragmentation techniques, high rate electron capture dissociation and infrared multiphoton dissociation. Simultaneous and consecutive irradiations of trapped ions with electrons and photons extended the possibilities for ion activation/dissociation reaction schemes and lead to improved peptide and protein characterization. Using these improvements, high rate electron capture dissociation was employed in time-limited experiments, such as liquid chromatography–tandem mass spectrometry and capillary electrophoresis-tandem mass spectrometry.

The analytical applications of the developed techniques have been demonstrated in top-down sequencing of peptides and proteins up to 29 kDa, improved sequencing of peptides with multiple disulfide bridges and secondary fragmentation (w-ion formation), as well as extended characterization of peptide mixtures separated by liquid chromatography and capillary electrophoresis. For instance, the dissociation of peptides resulting from enzymatic digestion of proteins provided complementary structural information on peptides and proteins, as well as their post-translational modifications.

Place, publisher, year, edition, pages
Uppsala: Acta Universitatis Upsaliensis, 2004. 66 p.
Series
Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology, ISSN 1104-232X ; 956
Keyword
Physics, mass spectrometry, Fourier transform ion cyclotron resonance, peptides and proteins, ion-electron interaction, electron capture dissociation, infrared multiphoton dissociation, liquid chromatography, capillary electrophoresis, Fysik
National Category
Physical Sciences
Identifiers
urn:nbn:se:uu:diva-4136 (URN)91-554-5917-X (ISBN)
Public defence
2004-04-23, Häggsalen, Ångström Laboratory, Lagerhydsvagen 1, Uppsala, 10:15 (English)
Opponent
Supervisors
Available from: 2004-03-25 Created: 2004-03-25 Last updated: 2011-03-21Bibliographically approved

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