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Protein Tertiary Structure by Crosslinking/Mass Spectrometry

Observing the structures of proteins within the cell and tracking structural changes under different cellular conditions are the ultimate challenges for structural biology. This, however, requires an experimental technique that can generate sufficient data for structure determination and is applicab...

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Detalles Bibliográficos
Autores principales: Schneider, Michael, Belsom, Adam, Rappsilber, Juri
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Trends Journals 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5854373/
https://www.ncbi.nlm.nih.gov/pubmed/29395654
http://dx.doi.org/10.1016/j.tibs.2017.12.006
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author Schneider, Michael
Belsom, Adam
Rappsilber, Juri
author_facet Schneider, Michael
Belsom, Adam
Rappsilber, Juri
author_sort Schneider, Michael
collection PubMed
description Observing the structures of proteins within the cell and tracking structural changes under different cellular conditions are the ultimate challenges for structural biology. This, however, requires an experimental technique that can generate sufficient data for structure determination and is applicable in the native environment of proteins. Crosslinking/mass spectrometry (CLMS) and protein structure determination have recently advanced to meet these requirements and crosslinking-driven de novo structure determination in native environments is now possible. In this opinion article, we highlight recent successes in the field of CLMS with protein structure modeling and challenges it still holds.
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spelling pubmed-58543732018-03-16 Protein Tertiary Structure by Crosslinking/Mass Spectrometry Schneider, Michael Belsom, Adam Rappsilber, Juri Trends Biochem Sci Article Observing the structures of proteins within the cell and tracking structural changes under different cellular conditions are the ultimate challenges for structural biology. This, however, requires an experimental technique that can generate sufficient data for structure determination and is applicable in the native environment of proteins. Crosslinking/mass spectrometry (CLMS) and protein structure determination have recently advanced to meet these requirements and crosslinking-driven de novo structure determination in native environments is now possible. In this opinion article, we highlight recent successes in the field of CLMS with protein structure modeling and challenges it still holds. Elsevier Trends Journals 2018-03 /pmc/articles/PMC5854373/ /pubmed/29395654 http://dx.doi.org/10.1016/j.tibs.2017.12.006 Text en © 2018 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Schneider, Michael
Belsom, Adam
Rappsilber, Juri
Protein Tertiary Structure by Crosslinking/Mass Spectrometry
title Protein Tertiary Structure by Crosslinking/Mass Spectrometry
title_full Protein Tertiary Structure by Crosslinking/Mass Spectrometry
title_fullStr Protein Tertiary Structure by Crosslinking/Mass Spectrometry
title_full_unstemmed Protein Tertiary Structure by Crosslinking/Mass Spectrometry
title_short Protein Tertiary Structure by Crosslinking/Mass Spectrometry
title_sort protein tertiary structure by crosslinking/mass spectrometry
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5854373/
https://www.ncbi.nlm.nih.gov/pubmed/29395654
http://dx.doi.org/10.1016/j.tibs.2017.12.006
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