Cited by 511Mass Spectrometry Techniques and ApplicationsAdvanced Proteomics Techniques and ApplicationsMetabolomics and Mass Spectrometry Studies

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High-Resolution Native Mass Spectrometry

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Tamara, Sem, den Boer, Maurits A., Heck, Albert J. R.·2022·Chemical Reviews

DOI 10.1021/acs.chemrev.1c00212PMC PMC9052423

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Abstract

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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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.
ORCID: Tamara, Sem
den Boer, Maurits A.
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
DOI: 10.1021/acs.chemrev.1c00212
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: cc-by-nc-nd
creativecommons.org/licenses/by-nc-nd/4.0/ (unspecified)
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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