Can Two-Dimensional IR-ECD Mass Spectrometry Improve Peptide de Novo Sequencing?
| Autor: | Maria A. van Agthoven, Lionel Chiron, Marc-André Delsuc, Tomos E. Morgan, Christopher A. Wootton, Mark P. Barrow, Alice M. Lynch, Peter B. O’Connor, Yuko P. Y. Lam |
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| Přispěvatelé: | Centre de Biochimie Structurale [Montpellier] (CBS), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM) |
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
chemistry.chemical_classification
[SDV.BIO]Life Sciences [q-bio]/Biotechnology Electron-capture dissociation Chemistry [SDV]Life Sciences [q-bio] 010401 analytical chemistry Analytical chemistry De novo peptide sequencing Peptide 010402 general chemistry Tandem mass spectrometry Mass spectrometry 01 natural sciences Fourier transform ion cyclotron resonance 0104 chemical sciences Analytical Chemistry Fragmentation (mass spectrometry) [CHIM.ANAL]Chemical Sciences/Analytical chemistry Mass spectrum [CHIM]Chemical Sciences ComputingMilieux_MISCELLANEOUS |
| Zdroj: | Analytical Chemistry Analytical Chemistry, American Chemical Society, 2018, 90 (5), pp.3496-3504. ⟨10.1021/acs.analchem.7b05324⟩ |
| ISSN: | 0003-2700 1520-6882 |
| Popis: | Two-dimensional mass spectrometry (2D MS) correlates precursor and fragment ions without ion isolation in a Fourier transform ion cyclotron resonance mass spectrometer (FTICR MS) for tandem mass spectrometry. Infrared activated electron capture dissociation (IR-ECD), using a hollow cathode configuration, generally yields more information for peptide sequencing in tandem mass spectrometry than ECD (electron capture dissociation) alone. The effects of the fragmentation zone on the 2D mass spectrum are investigated as well as the structural information that can be derived from it. The enhanced structural information gathered from the 2D mass spectrum is discussed in terms of how de novo peptide sequencing can be performed with increased confidence. 2D IR-ECD MS is shown to sequence peptides, to distinguish between leucine and isoleucine residues through the production of w ions as well as between C-terminal ( b/ c) and N-terminal ( y/ z) fragments through the use of higher harmonics, and to assign and locate peptide modifications. |
| Databáze: | OpenAIRE |
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