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High-Resolution Native Mass Spectrometry
Open accessAbstract
Native mass spectrometry (MS) involves the analysis and characterization of macromolecules, predominantly intact proteins and protein complexes, whereby as much as possible the native structural features of the analytes are retained. As such, native MS enables the study of secondary, tertiary, and even quaternary structure of proteins and other biomolecules. Native MS represents a relatively recent addition to the analytical toolbox of mass spectrometry and has over the past decade experienced immense growth, especially in enhancing sensitivity and resolving power but also in ease of use. With the advent of dedicated mass analyzers, sample preparation and separation approaches, targeted fragmentation techniques, and software solutions, the number of practitioners and novel applications has risen in both academia and industry. This review focuses on recent developments, particularly in high-resolution native MS, describing applications in the structural analysis of protein assemblies, proteoform profiling of─among others─biopharmaceuticals and plasma proteins, and quantitative and qualitative analysis of protein-ligand interactions, with the latter covering lipid, drug, and carbohydrate molecules, to name a few.
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“Native mass spectrometry has made significant advances over the last decade and has both been applied to analyze intact proteins and protein complexes which have been extensively reviewed.82,85”
From Connecting metabolome and phenotype: recent advances in functional metabolomics tools for the identification of bioactive natural products (2024) · cites this paper as [82]
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Keeping It Native: Non‐Denaturing Approaches to Top‐Down Protein Mass Spectrometry
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Metadata
- Authors
- Tamara, S., den Boer, M. A., & Heck, A. J. R.
- Affiliations
- Utrecht University (NL)
- Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH Utrecht, The Netherlands
- Corresponding author
- Heck, Albert J. R.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2021-08-20
- Volume
- 122
- Issue
- 8
- Pages
- 7269-7326
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- PMC
- PMC9052423
- OpenAlex
- W3194897413
- Cited by
- 511
- References
- 494
- Citations by year
- 2026: 95 · 2025: 138 · 2024: 123 · 2023: 95 · 2022: 54 · 2021: 6
- FWCI
- 7.75
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Chemical Reviews (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Funders
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NACTAR 16442, SPI.2017.028)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolomics and Mass Spectrometry Studies
- Keywords
- native mass spectrometry, high-resolution mass spectrometry, protein structure, protein complexes, protein assembly, biopharmaceuticals, plasma proteins, protein-ligand interactions, protein-lipid interactions, drug-protein interactions, carbohydrate-protein interactions, mass analyzers
- MeSH terms
- Ligands, Proteins, Mass Spectrometry, Macromolecular Substances
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