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A special issue of Essays in Biochemistry on structural mass spectrometry

Mass spectrometry (MS) is now established as an analytical tool to interrogate the structure and dynamics of proteins and their assemblies. An array of MS-based technologies has been developed, with each providing unique information pertaining to protein structure, and forming the heart of integrati...

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Detalles Bibliográficos
Autores principales: Britt, Hannah M., Beveridge, Rebecca, Calabrese, Antonio N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10070473/
https://www.ncbi.nlm.nih.gov/pubmed/36988080
http://dx.doi.org/10.1042/EBC20230006
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author Britt, Hannah M.
Beveridge, Rebecca
Calabrese, Antonio N.
author_facet Britt, Hannah M.
Beveridge, Rebecca
Calabrese, Antonio N.
author_sort Britt, Hannah M.
collection PubMed
description Mass spectrometry (MS) is now established as an analytical tool to interrogate the structure and dynamics of proteins and their assemblies. An array of MS-based technologies has been developed, with each providing unique information pertaining to protein structure, and forming the heart of integrative structural biology studies. This special issue includes a collection of review articles that discuss both established and emerging structural MS methodologies, along with examples of how these technologies are being deployed to interrogate protein structure and function. Combined, this collection highlights the immense potential of the structural MS toolkit in the study of molecular mechanisms underpinning cellular homeostasis and disease.
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spelling pubmed-100704732023-04-05 A special issue of Essays in Biochemistry on structural mass spectrometry Britt, Hannah M. Beveridge, Rebecca Calabrese, Antonio N. Essays Biochem Biochemical Techniques & Resources Mass spectrometry (MS) is now established as an analytical tool to interrogate the structure and dynamics of proteins and their assemblies. An array of MS-based technologies has been developed, with each providing unique information pertaining to protein structure, and forming the heart of integrative structural biology studies. This special issue includes a collection of review articles that discuss both established and emerging structural MS methodologies, along with examples of how these technologies are being deployed to interrogate protein structure and function. Combined, this collection highlights the immense potential of the structural MS toolkit in the study of molecular mechanisms underpinning cellular homeostasis and disease. Portland Press Ltd. 2023-03 2023-03-29 /pmc/articles/PMC10070473/ /pubmed/36988080 http://dx.doi.org/10.1042/EBC20230006 Text en © 2023 The Author(s). https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) . Open access for the present article was enabled by the participation of University of Leeds in an all-inclusive Read & Publish agreement with Portland Press and the Biochemical Society under a transformative agreement with JISC.
spellingShingle Biochemical Techniques & Resources
Britt, Hannah M.
Beveridge, Rebecca
Calabrese, Antonio N.
A special issue of Essays in Biochemistry on structural mass spectrometry
title A special issue of Essays in Biochemistry on structural mass spectrometry
title_full A special issue of Essays in Biochemistry on structural mass spectrometry
title_fullStr A special issue of Essays in Biochemistry on structural mass spectrometry
title_full_unstemmed A special issue of Essays in Biochemistry on structural mass spectrometry
title_short A special issue of Essays in Biochemistry on structural mass spectrometry
title_sort special issue of essays in biochemistry on structural mass spectrometry
topic Biochemical Techniques & Resources
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10070473/
https://www.ncbi.nlm.nih.gov/pubmed/36988080
http://dx.doi.org/10.1042/EBC20230006
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