Complementary Benzophenone Cross-Linking/Mass Spectrometry Photochemistry

Adam Belsom; Gemma Mudd; Sven Giese; Manfred Auer; Juri Rappsilber

doi:10.1021/acs.analchem.6b04938

Complementary Benzophenone Cross-Linking/Mass Spectrometry Photochemistry

Adam Belsom, Gemma Mudd, Sven Giese, Manfred Auer, Juri Rappsilber

School of Biological Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

Use of a heterobifunctional photoactivatable cross-linker, sulfo-SDA (diazirine), has yielded high-density data that facilitated structure modeling of individual proteins. We expand the photoactivatable chemistry toolbox here with a second reagent, sulfo-SBP (benzophenone). This further increases the density of photo-cross-linking to a factor of 20× over conventional cross-linking. Importantly, the two different photoactivatable groups display orthogonal directionality, enabling access to different protein regions, unreachable with a single cross-linker.

Original language	English
Pages (from-to)	5319-5324
Number of pages	6
Journal	Analytical Chemistry
Volume	89
Issue number	10
Early online date	21 Apr 2017
DOIs	https://doi.org/10.1021/acs.analchem.6b04938 https://doi.org/10.1021/acs.analchem.6b04938
Publication status	Published - 16 May 2017

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Journal Article

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Final published version, 445 KBLicence: Creative Commons: Attribution (CC-BY)
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ACS AuthorChoice - This is an open access article published under a Creative Commons Attribution (CC-BY) License, which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
Final published version, 2.66 MBLicence: Creative Commons: Attribution (CC-BY)

Wellcome Centre for Cell Biology
Tollervey, D. (Principal Investigator)
UK-based charities
1/12/16 → 1/12/21
Project: Research
Proteomics at the Wellcome Trust Centre for Cell Biology (WTCCB) and School of Biological Sciences (SBS), Edinburgh
Rappsilber, J. (Principal Investigator)
UK-based charities
1/10/15 → 30/09/20
Project: Research
Protein structures in the context of time and space by mass spectrometry
Rappsilber, J. (Principal Investigator)
UK-based charities
1/06/14 → 31/05/21
Project: Research

Cite this

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AU - Auer, Manfred

AU - Rappsilber, Juri

PY - 2017/5/16

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AB - Use of a heterobifunctional photoactivatable cross-linker, sulfo-SDA (diazirine), has yielded high-density data that facilitated structure modeling of individual proteins. We expand the photoactivatable chemistry toolbox here with a second reagent, sulfo-SBP (benzophenone). This further increases the density of photo-cross-linking to a factor of 20× over conventional cross-linking. Importantly, the two different photoactivatable groups display orthogonal directionality, enabling access to different protein regions, unreachable with a single cross-linker.

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Complementary Benzophenone Cross-Linking/Mass Spectrometry Photochemistry

Abstract

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Projects

Wellcome Centre for Cell Biology

Proteomics at the Wellcome Trust Centre for Cell Biology (WTCCB) and School of Biological Sciences (SBS), Edinburgh

Protein structures in the context of time and space by mass spectrometry

Cite this