The evolving contribution of mass spectrometry to integrative structural biology
Open accessAbstract
Protein complexes are key catalysts and regulators for the majority of cellular processes. Unveiling their assembly and structure is essential to understanding their function and mechanism of action. Although conventional structural techniques such as X-ray crystallography and NMR have solved the structure of important protein complexes, they cannot consistently deal with dynamic and heterogeneous assemblies, limiting their applications to small scale experiments. A novel methodological paradigm, integrative structural biology, aims at overcoming such limitations by combining complementary data sources into a comprehensive structural model. Recent applications have shown that a range of mass spectrometry (MS) techniques are able to generate interaction and spatial restraints (cross-linking MS) information on native complexes or to study the stoichiometry and connectivity of entire assemblies (native MS) rapidly, reliably, and from small amounts of substrate. Although these techniques by themselves do not solve structures, they do provide invaluable structural information and are thus ideally suited to contribute to integrative modeling efforts. The group of Brian Chait has made seminal contributions in the use of mass spectrometric techniques to study protein complexes. In this perspective, we honor the contributions of the Chait group and discuss concepts and milestones of integrative structural biology. We also review recent examples of integration of structural MS techniques with an emphasis on cross-linking MS. We then speculate on future MS applications that would unravel the dynamic nature of protein complexes upon diverse cellular states. Graphical Abstract ᅟ.
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Complementary measurement techniques are beneficial and may ultimately be necessary to gain a full understanding of biological structure across multiple scales.
“A core concept is that complementary measurement techniques are not only beneficial in general, but they may ultimately be necessary to gain a full understanding of biological structure across multiple scales.”
From Mapping the multiscale structure of biological systems (2021) · cites this paper as Faini et al., 2016
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Swati, B., Sýs, J., Machara, A., Petra, J., & Martin, H. (2024) · Journal of Proteomics · doi:10.1016/j.jprot.2024.105330 · Cited by 3 · see citing works
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Ohlendieck, K. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7268-5_9 · Cited by 3 · see citing works
Overview Update: Computational Prediction of Intrinsic Disorder in Proteins
Uversky, V. N., & Kurgan, L. (2023) · Current Protocols · doi:10.1002/cpz1.802 · Cited by 4 · see citing works
Advanced Technologies for Protein Complex Production and Characterization
Vega, M. C., & Fernández, F. J. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-52193-5 · Cited by 3 · see citing works
Reporting on the future of integrative structural biology ORAU workshop
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Cross‐linking Applications in Structural Proteomics
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Proteome-scale studies of protein stability
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- Authors
- Faini, M., Stengel, F., & Aebersold, R.
- Affiliations
- ETH Zurich (CH)
- University of Konstanz (DE)
- University of Zurich (CH)
- Corresponding author
- Aebersold, Ruedi
- Venue
- Journal of the American Society for Mass Spectrometry
- Publisher
- American Chemical Society (ACS)
- Published
- 2016-04-07
- Volume
- 27
- Issue
- 6
- Pages
- 966-974
- ISSN
- 1044-0305 (ISSN-L)
- PMC
- PMC4867889
- OpenAlex
- W2330858956
- Cited by
- 44
- References
- 66
- Citations by year
- 2026: 1 · 2024: 3 · 2023: 1 · 2022: 3 · 2021: 7 · 2020: 10 · 2019: 7 · 2018: 4 · 2017: 5 · 2016: 3
- FWCI
- 0.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Journal of the American Society for Mass Spectrometry (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- KOPS (University of Konstanz) (submittedVersion, cc-by)
- Repository for Publications and Research Data (ETH Zurich) (submittedVersion, cc-by)
- ETH Zürich Research Collection (cc-by)
- Funders
- European Commission (201648, 233226, 115366)
- H2020 European Research Council (670821)
- FP7 Ideas: European Research Council (233226)
- 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 › Protein Structure and Dynamics
- Keywords
- integrative structural biology, protein complexes, cross-linking mass spectrometry, native mass spectrometry, protein complex formation, stoichiometry, structural modeling
- MeSH terms
- Models, Molecular, Magnetic Resonance Spectroscopy, Proteins, Mass Spectrometry
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