Fast atom bombardment for peptide sequencing - a comparison with conventional ionization techniques

König, Wilfried Α.; Aydin, Mitat; Schulze, Uwe; Rapp, U.; Höhn, M.; Pesch, R.; Kalikhevitch, V.N.

doi:10.1016/0020-7381(83)80137-5

Cited by 26 publications

(3 citation statements)

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“…With the advent of soft ionization techniques, tandem mass spectrometry (MS/MS) as a source for sequence information of peptides and proteins has superseded classical Edman sequencing almost completely. While in the beginning electron ionization1–4 (EI) or fast‐atom bombardment5–8 (FAB) was widely used, these techniques had significant limitations regarding required derivatization of the samples or the peptide size which could be analyzed. With the introduction of ESI by Fenn et al .,9–11 this technique, in combination with MS/MS by triple quadrupole, ion trap or quadrupole‐time‐of‐flight (Q‐TOF), became the most widely used source of mass spectrometric sequence information from peptides and proteins.…”

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confidence: 99%

Comparison of laser‐induced dissociation and high‐energy collision‐induced dissociation using matrix‐assisted laser desorption/ionization tandem time‐of‐flight (MALDI‐TOF/TOF) for peptide and protein identification

Macht

Asperger

Deininger

2004

Rapid Comm Mass Spectrometry

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The fragmentation of peptides under laser-induced dissociation (LID) as well as high-energy collision-induced dissociation (CID) conditions has been investigated. The effect of the different fragmentation mechanisms on the formation of specific fragment ion types and the usability of the resulting spectra, e.g. for high-throughput protein identification, has been evaluated. Also, basic investigations on the influence of the matrix, as well as laser fluence, on the fragment ion formation and the consequences in the spectral appearance are discussed. The preconditions for obtaining 'pure' CID spectra on matrix-assisted laser desorption/ionization tandem time-of-flight (MALDI-TOF/TOF) instruments are evaluated and discussed as well as the differences between LID and CID in the resulting fragment ion types. While containing a wealth of information due to additional fragment ions in comparison with LID, CID spectra are significantly more complex than LID spectra and, due to different fragmentation patterns, the CID spectra are of limited use for protein identification, even under optimized parameter settings, due to significantly lower scores for the individual spectra. Conditions for optimal results regarding protein identification using MALDI-TOF/TOF instruments have been evaluated. For database searches using tandem mass spectrometric data, the use of LID as fragmentation technique in combination with parameter settings supporting the use of internal fragment ions turned out to yield the optimal results.

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confidence: 99%

Comparison of laser‐induced dissociation and high‐energy collision‐induced dissociation using matrix‐assisted laser desorption/ionization tandem time‐of‐flight (MALDI‐TOF/TOF) for peptide and protein identification

Macht

Asperger

Deininger

2004

Rapid Comm Mass Spectrometry

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“…At first, all the subsequences composed of three amino acids, 18 x 18 x 18 in number, such as 'GGG, 'GGA', 'GGS', . .…”

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confidence: 99%

Computer-aided peptide sequencing by fast atom bombardment mass spectrometry

Ishikawa

Niwa

1986

Biol. Mass Spectrom.

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This paper proposes an efficient method for computer-aided peptide sequencing based on fast atom bombardment mass spectrometry. The method allows us to analyse peptides much larger than loo0 u within a reasonable cpu time and to have a set of amino acid sequences which are consistent with the observed fast atom bombardment mass spectrum to varying degrees. Another feature is that there is no need to pick sequence ion peaks out of the spectrum; all the ions observed are equally taken into account in the analysis so that one can exhaust the possibilities expected from the whole spectrum. For most samples of penta-to tridecapeptides, parts of an amino acid sequence could he reproduced satisfactorily without prior knowledge of amino acid composition. The degree of success in sequence elucidation depends entirely on the spectrum used in the analysis. When fragment ion peaks are clearly observed, the sequence can be predicted successfully. The result obtained for a given amino acid composition was always satisfactory.

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“…The most commonly observed fragment series are A, B, C", Y", Z, and Z" for positive ion spectra (19.78-81) and C, "X, Y, "Y, and Z for negative ion spectra (19,80,81). It is unusual for all series to be present in the spectrum of a peptide, and the factors that determine which series will dominate are not well understood.…”

Section: Fragment-ion Seriesmentioning

confidence: 99%

Methods of Protein Microcharacterization

Shively¹

1986

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Fast atom bombardment for peptide sequencing - a comparison with conventional ionization techniques

Cited by 26 publications

References 2 publications

Comparison of laser‐induced dissociation and high‐energy collision‐induced dissociation using matrix‐assisted laser desorption/ionization tandem time‐of‐flight (MALDI‐TOF/TOF) for peptide and protein identification

Comparison of laser‐induced dissociation and high‐energy collision‐induced dissociation using matrix‐assisted laser desorption/ionization tandem time‐of‐flight (MALDI‐TOF/TOF) for peptide and protein identification

Computer-aided peptide sequencing by fast atom bombardment mass spectrometry

Methods of Protein Microcharacterization

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