Cited by 901Mass Spectrometry Techniques and ApplicationsProtein Structure and DynamicsMolecular Spectroscopy and Structure

The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics

Lanucara, Francesco, Holman, Stephen W., Gray, Christopher J., Eyers, Claire E.·2014·Nature Chemistry

Abstract

Mass spectrometry is a vital tool for molecular characterization, and the allied technique of ion mobility is enhancing many areas of (bio)chemical analysis. Strong synergy arises between these two techniques because of their ability to ascertain complementary information about gas-phase ions. Ion mobility separates ions (from small molecules up to megadalton protein complexes) based on their differential mobility through a buffer gas. Ion mobility-mass spectrometry (IM-MS) can thus act as a tool to separate complex mixtures, to resolve ions that may be indistinguishable by mass spectrometry alone, or to determine structural information (for example rotationally averaged cross-sectional area), complementary to more traditional structural approaches. Finally, IM-MS can be used to gain insights into the conformational dynamics of a system, offering a unique means of characterizing flexibility and folding mechanisms. This Review critically describes how IM-MS has been used to enhance various areas of chemical and biophysical analysis.

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Crossref · 10.1038/nchem.1889

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  • IM-MS correlates with known protein structure.

    “Previous studies have shown that IM-MS correlates with known protein structure,”
  • Ion mobility experiments show that the overall 3D shape of proteins, especially in the lower charge states naturally generated by ESI from non-denaturing solutions, is usually consistent with structures obtained from X-ray diffraction and nuclear magnetic resonance (although exceptions exist).

    “Ion mobility experiments show that the overall 3D shape of proteins – especially in the lower charge states naturally generated by ESI from non-denaturing solutions – is usually consistent with structures obtained from X-ray diffraction (XRD) and nuclear magnetic resonance (NMR) (although exceptions exist).”

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Authors
Lanucara, F., Holman, S. W., Gray, C. J., & Eyers, C. E.
Affiliations
  • University of Liverpool (GB)
  • University of Manchester (GB)
Corresponding author
Eyers, Claire E.
Venue
Nature Chemistry
Published
2014-03-21
Volume
6
Issue
4
Pages
281-294
ISSN
  • 1755-4330 (ISSN-L)
  • 1755-4349
OpenAlex
W1992505804
Cited by
901
References
163
Citations by year
2026: 28 · 2025: 58 · 2024: 50 · 2023: 60 · 2022: 67 · 2021: 79 · 2020: 92 · 2019: 92 · 2018: 100 · 2017: 108 · 2016: 85 · 2015: 56 · 2014: 24
FWCI
8.79
Type
journal article
Language
en
Open access
closed
Locations
  • Nature Chemistry (publishedVersion)
  • PubMed (publishedVersion)
  • Research Explorer (The University of Manchester) (submittedVersion)
Funders
  • European Commission
  • Biotechnology and Biological Sciences Research Council (BB/H007113/1, BB/F00561X/1, BB/G009058/1)
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 › Molecular Spectroscopy and Structure
Keywords
ion mobility mass spectrometry, structural characterization, conformational dynamics, cross-sectional area, complex mixtures, protein flexibility, protein folding mechanism, molecular characterization
MeSH terms
Biophysics, Ions, Molecular Conformation, Mass Spectrometry

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