Cited by 72Mass Spectrometry Techniques and ApplicationsProtein Structure and DynamicsAdvanced Proteomics Techniques and Applications

Unique insights to intrinsically disordered proteins provided by ion mobility mass spectrometry

Stuchfield, Dale, Barran, Perdita·2018·Current Opinion in Chemical Biology

Abstract

Entire functional proteins as well as large regions of proteins lack structural elements which are resolvable via crystallography or NMR. These intrinsically disordered proteins (IDPs) or regions (IDRs) are often involved in cell regulation processes, for example in signalling hubs and as a result aberrant behaviour can cause or be representative of disease. As a consequence there is a pressing need to develop alternative structural methods for IDPs and the interactions that they may form with other proteins and/or with potential inhibitors of binding. One such method is ion mobility mass spectrometry (IM-MS) coupled with careful application of electrospray ionisation, which shows great promise as a technique that does not 'care' if a protein is structured or not. We highlight recent work which has employed IM-MS to study conformational heterogeneity in disordered proteins, and discuss the opportunities, as well as the challenges of this approach.

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Crossref · 10.1016/j.cbpa.2018.01.007

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  • Many challenging analytes such as membrane proteins, intrinsically disordered proteins, highly dynamic or heterogeneous complexes, or very large systems such as intact virus capsids can all be investigated using native MS, as well as their associated proteoforms.

    “By using appropriate sample preparation, ionisation conditions, and instrumentation, many challenging analytes such as membrane proteins,18,42 intrinsically disordered proteins,43 highly dynamic or heterogeneous complexes,19 or very large systems such as intact virus capsids44 can all be investigated using native MS, as well as their associated proteoforms.45”

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Authors
Stuchfield, D., & Barran, P.
Affiliations
University of Manchester (GB)
Corresponding author
Barran, Perdita
Venue
Current Opinion in Chemical Biology
Publisher
Elsevier BV
Published
2018-02
Volume
42
Pages
177-185
ISSN
1367-5931 (ISSN-L)
OpenAlex
W2791942866
Cited by
72
References
69
Citations by year
2026: 5 · 2025: 5 · 2024: 5 · 2023: 12 · 2022: 11 · 2021: 8 · 2020: 6 · 2019: 13 · 2018: 7
FWCI
1.07
Type
journal article
Language
en
Open access
closed
Locations
  • Current Opinion in Chemical Biology (publishedVersion)
  • PubMed (publishedVersion)
  • Research Explorer (The University of Manchester) (submittedVersion)
Topics
  • Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Keywords
intrinsically disordered proteins, intrinsically disordered regions, ion mobility mass spectrometry, electrospray ionization, conformational heterogeneity, protein structure determination, protein-protein interaction, cell regulation
MeSH terms
Ion Mobility Spectrometry, Models, Molecular, Protein Conformation, Signal Transduction, Spectrometry, Mass, Electrospray Ionization, Intrinsically Disordered Proteins

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