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PreprintCited by 2Mass Spectrometry Techniques and ApplicationsAdvanced Proteomics Techniques and ApplicationsProtein Structure and Dynamics

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Isobaric crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and complexes

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Luo, Jie, Ranish, Jeff·2022·eLife
DOI 10.1101/2022.12.02.518925

Preprint — published as 10.7554/elife.99809.3 · Paper page

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Abstract

Dynamic conformational and structural changes in proteins and protein complexes play a central and ubiquitous role in the regulation of protein function, yet it is very challenging to study these changes, especially for large protein complexes, under physiological conditions. Here we introduce a novel isobaric crosslinker, Qlinker, for studying conformational and structural changes in proteins and protein complexes using quantitative crosslinking mass spectrometry (qCLMS). Qlinkers are small and simple, amine-reactive molecules with an optimal extended distance of ∼10 Å which use MS2 reporter ions for relative quantification of Qlinker-modified peptides derived from different samples. We synthesized the 2-plex Q2linker and showed that the Q2linker can provide quantitative crosslinking data that pinpoints key conformational and structural changes in biosensors, binary and ternary complexes composed of the general transcription factors TBP, TFIIA, and TFIIB, and RNA polymerase II (pol II) complexes.

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Metadata

Authors
Luo, J., & Ranish, J.
Affiliations
Institute for Systems Biology (US)
ORCID
Venue
eLife
Publisher
openRxiv
Published
2022-12-05
Volume
13
ISSN
2050-084X (ISSN-L)
DOI
10.1101/2022.12.02.518925
OpenAlex
W4404376995
Cited by
2
References
1
Citations by year
2025: 2
FWCI
0.25
Type
journal article
Language
en
Open access
Licence
Locations
  • eLife (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
Funders
  • National Institutes of Health
  • National Institute of General Medical Sciences (R01GM108908, R01GM136974, R01GM144559)
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
protein conformational change, protein complexes, transcription factor complex, TATA-binding protein, TFIIA, TFIIB, RNA polymerase II, biosensors, ternary complex

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CoChat. (2026). Citation check: Isobaric crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and complexes. https://app.cochat.ai/papers/10.1101/2022.12.02.518925
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Luo, J., & Ranish, J. (2022). Isobaric crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and complexes. eLife. https://doi.org/10.1101/2022.12.02.518925