Exploring the structure and dynamics of macromolecular complexes by native mass spectrometry
| Autor: | Luca Signor, Elisabetta Boeri Erba, Carlo Petosa |
|---|---|
| Přispěvatelé: | Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017) |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Macromolecular Substances Biophysics Protein-ligand interactions Mass spectrometry Ligands Biochemistry Mass Spectrometry 03 medical and health sciences Three dimensional architecture Integrative structural biology Native top-down MS chemistry.chemical_classification 030102 biochemistry & molecular biology Fourier Analysis [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Biomolecule Stoichiometry 030104 developmental biology chemistry Structural biology Covalent bond Macromolecular complexes Macromolecular Complexes 2D interaction map Native mass spectrometry (MS) |
| Zdroj: | Journal of Proteomics Journal of Proteomics, Elsevier, 2020, 222, pp.103799. ⟨10.1016/j.jprot.2020.103799⟩ Journal of Proteomics, 2020, 222, pp.103799. ⟨10.1016/j.jprot.2020.103799⟩ |
| ISSN: | 1874-3919 1876-7737 |
| DOI: | 10.1016/j.jprot.2020.103799⟩ |
| Popis: | International audience; Mass spectrometry (MS) is an effective approach for determining the mass of biomolecules with high accuracy, sensitivity and speed. Over the past 25 years, MS performed under non-denaturing conditions ("native MS") has been successfully exploited to investigate non-covalently associated biomolecules. Here we illustrate native MS applications aimed at studying protein-ligand interactions and structures of biomolecular assemblies, including both soluble and membrane protein complexes. Moreover, we review how the partial dissociation of holo-complexes can be used to determine the stoichiometry of subunits and their topology. We also describe "native top-down MS", an approach based on Fourier Transform MS (FT MS), whereby non-covalent interactions are preserved while covalent bonds are selectively fragmented. Overall, native MS plays an increasingly important role in integrative structural biology, helping researchers to elucidate the three dimensional architecture of intricate macromolecular complexes. |
| Databáze: | OpenAIRE |
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