Publikation: Affinity-Mass Spectrometry Approaches for Elucidating Structures and Interactions of Protein-Ligand Complexes
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2014
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WOODS, Alisa G., ed., Costel C. DARIE, ed.. Advancements of Mass Spectrometry in Biomedical Research. Cham: Springer, 2014, pp. 129-151. Advances in Experimental Medicine and Biology. 806. ISBN 978-3-319-06067-5. Available under: doi: 10.1007/978-3-319-06068-2_7
Zusammenfassung
Affinity-based approaches in combination with mass spectrometry for molecular structure identification in biological complexes such as protein-protein, and protein-carbohydrate complexes have become popular in recent years. Affinity-mass spectrometry involves immobilization of a biomolecule on a chemically activated support, affinity binding of ligand(s), dissociation of the complex, and mass spectrometric analysis of the bound fraction. In this chapter the affinity-mass spectrometric methodologies will be presented for (1) identification of the epitope structures in the Abeta amyloid peptide, (2) identification of oxidative modifications in proteins such as nitration of tyrosine, (3) determination of carbohydrate recognition domains, and as (4) development of a biosensor chip-based mass spectrometric system for concomitant quantification and identification of protein-ligand complexes.
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540 Chemie
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Surface Acoustic Wave, Tryptic Peptide, Eosinophil Cationic Protein, Elution Fraction, Carbohydrate Recognition Domain
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PETRE, Brînduşa-Alina, 2014. Affinity-Mass Spectrometry Approaches for Elucidating Structures and Interactions of Protein-Ligand Complexes. In: WOODS, Alisa G., ed., Costel C. DARIE, ed.. Advancements of Mass Spectrometry in Biomedical Research. Cham: Springer, 2014, pp. 129-151. Advances in Experimental Medicine and Biology. 806. ISBN 978-3-319-06067-5. Available under: doi: 10.1007/978-3-319-06068-2_7BibTex
@incollection{Petre2014Affin-41796,
year={2014},
doi={10.1007/978-3-319-06068-2_7},
title={Affinity-Mass Spectrometry Approaches for Elucidating Structures and Interactions of Protein-Ligand Complexes},
number={806},
isbn={978-3-319-06067-5},
publisher={Springer},
address={Cham},
series={Advances in Experimental Medicine and Biology},
booktitle={Advancements of Mass Spectrometry in Biomedical Research},
pages={129--151},
editor={Woods, Alisa G. and Darie, Costel C.},
author={Petre, Brînduşa-Alina}
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<dcterms:abstract xml:lang="eng">Affinity-based approaches in combination with mass spectrometry for molecular structure identification in biological complexes such as protein-protein, and protein-carbohydrate complexes have become popular in recent years. Affinity-mass spectrometry involves immobilization of a biomolecule on a chemically activated support, affinity binding of ligand(s), dissociation of the complex, and mass spectrometric analysis of the bound fraction. In this chapter the affinity-mass spectrometric methodologies will be presented for (1) identification of the epitope structures in the Abeta amyloid peptide, (2) identification of oxidative modifications in proteins such as nitration of tyrosine, (3) determination of carbohydrate recognition domains, and as (4) development of a biosensor chip-based mass spectrometric system for concomitant quantification and identification of protein-ligand complexes.</dcterms:abstract>
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