Cornwell, O and Ault, JR orcid.org/0000-0002-5131-438X (2022) Fast photochemical oxidation of proteins coupled with mass spectrometry. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1870 (9). 140829. ISSN 1570-9639
Abstract
Fast photochemical oxidation of proteins (FPOP) is a hydroxyl radical footprinting approach whereby radicals, produced by UV laser photolysis of hydrogen peroxide, induce oxidation of amino acid side-chains. Mass Spectrometry (MS) is employed to locate and quantify the resulting irreversible, covalent oxidations to use as a surrogate for side-chain solvent accessibility. Modulation of oxidation levels under different conditions allows for the characterisation of protein conformation, dynamics and binding epitopes. FPOP has been applied to structurally diverse and biopharmaceutically relevant systems from small, monomeric aggregation-prone proteins to proteome-wide analysis of whole organisms. This review evaluates the current state of FPOP, the progress needed to address data analysis bottlenecks, particularly for residue-level analysis, and highlights significant developments of the FPOP platform that have enabled its versatility and complementarity to other structural biology techniques.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2022 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/bync-nd/4.0/). |
Keywords: | Fast photochemical oxidation of proteins; Structural proteomics; Hydroxyradical footprinting; Mass spectrometry |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Biomolecular Mass Spectroscopy (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 14 Dec 2022 15:31 |
Last Modified: | 14 Dec 2022 15:31 |
Status: | Published |
Publisher: | Elsevier BV |
Identification Number: | 10.1016/j.bbapap.2022.140829 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:193933 |