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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Trends Journals
2018
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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. |
format | Online Article Text |
id | pubmed-5854373 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Elsevier Trends Journals |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT schneidermichael proteintertiarystructurebycrosslinkingmassspectrometry AT belsomadam proteintertiarystructurebycrosslinkingmassspectrometry AT rappsilberjuri proteintertiarystructurebycrosslinkingmassspectrometry |