Protein Footprinting with Radical Probe Mass Spectrometry- Two Decades of Achievement

Maleknia, SD; Downard, KM

Protein Footprinting with Radical Probe Mass Spectrometry- Two Decades of Achievement

Maleknia, SD Downard, KM

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Publisher:: Bentham Science Publishers Ltd.
Publication Type:: Journal Article
Citation:: Protein & Peptide Letters, 2019, 26 (1), pp. 4 - 15
Issue Date:: 2019-02-13

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Field	Value	Language
dc.contributor.author	Maleknia, SD	en_US
dc.contributor.author	Downard, KM	en_US
dc.date.issued	2019-02-13	en_US
dc.identifier.citation	Protein & Peptide Letters, 2019, 26 (1), pp. 4 - 15	en_US
dc.identifier.issn	0929-8665	en_US
dc.identifier.uri	http://hdl.handle.net/10453/131310
dc.description.abstract	<jats:sec> <jats:title>Background:</jats:title> <jats:p> Radical Probe Mass Spectrometry (RP-MS) describes a pioneering methodology in structural biology that enables the study of protein structures, their interactions, and dynamics on fast timescales (down to sub-milliseconds). Hydroxyl radicals (•OH) generated directly from water within aqueous solutions induce the oxidation of reactive, solvent accessible amino acid side chains that are then analyzed by mass spectrometry. Introduced in 1998 at the American Society for Mass Spectrometry annual conference, RP-MS was first published on in 1999. </jats:p></jats:sec> <jats:sec> <jats:title>Objective:</jats:title> <jats:p> This review article describes developments and applications of the RP-MS methodology over the past two decades. </jats:p></jats:sec> <jats:sec> <jats:title>Methods:</jats:title> <jats:p> The RP-MS method has been variously referred to as synchrotron X-ray radiolysis footprinting, Hydroxyl Radical Protein Footprinting (HRPF), X-ray Footprinting with Mass Spectrometry (XF-MS), Fast Photochemical Oxidation of Proteins (FPOP), oxidative labelling, covalent oxidative labelling, and even the Stability of Proteins from Rates of Oxidation (SPROX). </jats:p></jats:sec> <jats:sec> <jats:title>Results:</jats:title> <jats:p>The article describes the utility of hydroxyl radicals as a protein structural probe, the advantages of RP-MS in comparison to other MS-based approaches, its proof of concept using ion mobility mass spectrometry, its application to protein structure, folding, complex and aggregation studies, its extension to study the onset of protein damage, its implementation using a high throughput sample loading approach, and the development of protein docking algorithms to aid with data analysis and visualization. </jats:p></jats:sec> <jats:sec> <jats:title>Conclusion:</jats:title> <jats:p> RP-MS represents a powerful new structural approach that can aid in our understanding of the structure and functions of proteins, and the impact of sustained oxidation on proteins in disease pathogenesis.</jats:p></jats:sec>	en_US
dc.language	en	en_US
dc.publisher	Bentham Science Publishers Ltd.	en_US
dc.relation.ispartof	Protein & Peptide Letters	en_US
dc.relation.isbasedon	10.2174/0929866526666181128124241	en_US
dc.subject.classification	Biophysics	en_US
dc.title	Protein Footprinting with Radical Probe Mass Spectrometry- Two Decades of Achievement	en_US
dc.type	Journal Article
utslib.citation.volume	1	en_US
utslib.citation.volume	26	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	0304 Medicinal and Biomolecular Chemistry	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Mathematical and Physical Sciences
utslib.copyright.status	closed_access
pubs.consider-herdc	false	en_US
pubs.issue	1	en_US
pubs.publication-status	Published	en_US
pubs.volume	26	en_US

Abstract:

Background: Radical Probe Mass Spectrometry (RP-MS) describes a pioneering methodology in structural biology that enables the study of protein structures, their interactions, and dynamics on fast timescales (down to sub-milliseconds). Hydroxyl radicals (•OH) generated directly from water within aqueous solutions induce the oxidation of reactive, solvent accessible amino acid side chains that are then analyzed by mass spectrometry. Introduced in 1998 at the American Society for Mass Spectrometry annual conference, RP-MS was first published on in 1999. Objective: This review article describes developments and applications of the RP-MS methodology over the past two decades. Methods: The RP-MS method has been variously referred to as synchrotron X-ray radiolysis footprinting, Hydroxyl Radical Protein Footprinting (HRPF), X-ray Footprinting with Mass Spectrometry (XF-MS), Fast Photochemical Oxidation of Proteins (FPOP), oxidative labelling, covalent oxidative labelling, and even the Stability of Proteins from Rates of Oxidation (SPROX). Results: The article describes the utility of hydroxyl radicals as a protein structural probe, the advantages of RP-MS in comparison to other MS-based approaches, its proof of concept using ion mobility mass spectrometry, its application to protein structure, folding, complex and aggregation studies, its extension to study the onset of protein damage, its implementation using a high throughput sample loading approach, and the development of protein docking algorithms to aid with data analysis and visualization. Conclusion: RP-MS represents a powerful new structural approach that can aid in our understanding of the structure and functions of proteins, and the impact of sustained oxidation on proteins in disease pathogenesis.

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http://hdl.handle.net/10453/131310