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Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry
Recent advances in protein mass spectrometry (MS) have enabled determinations of hydrogen deuterium exchange (HDX) in large macromolecular complexes. HDX-MS became a valuable tool to follow protein folding, assembly and aggregation. The methodology has a wide range of applications in biotechnology r...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2008
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2365927/ https://www.ncbi.nlm.nih.gov/pubmed/18394161 http://dx.doi.org/10.1186/1475-2859-7-12 |
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author | Suchanova, Bohumila Tuma, Roman |
author_facet | Suchanova, Bohumila Tuma, Roman |
author_sort | Suchanova, Bohumila |
collection | PubMed |
description | Recent advances in protein mass spectrometry (MS) have enabled determinations of hydrogen deuterium exchange (HDX) in large macromolecular complexes. HDX-MS became a valuable tool to follow protein folding, assembly and aggregation. The methodology has a wide range of applications in biotechnology ranging from quality control for over-expressed proteins and their complexes to screening of potential ligands and inhibitors. This review provides an introduction to protein folding and assembly followed by the principles of HDX and MS detection, and concludes with selected examples of applications that might be of interest to the biotechnology community. |
format | Text |
id | pubmed-2365927 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-23659272008-05-03 Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry Suchanova, Bohumila Tuma, Roman Microb Cell Fact Review Recent advances in protein mass spectrometry (MS) have enabled determinations of hydrogen deuterium exchange (HDX) in large macromolecular complexes. HDX-MS became a valuable tool to follow protein folding, assembly and aggregation. The methodology has a wide range of applications in biotechnology ranging from quality control for over-expressed proteins and their complexes to screening of potential ligands and inhibitors. This review provides an introduction to protein folding and assembly followed by the principles of HDX and MS detection, and concludes with selected examples of applications that might be of interest to the biotechnology community. BioMed Central 2008-04-04 /pmc/articles/PMC2365927/ /pubmed/18394161 http://dx.doi.org/10.1186/1475-2859-7-12 Text en Copyright © 2008 Suchanova and Tuma; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Suchanova, Bohumila Tuma, Roman Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry |
title | Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry |
title_full | Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry |
title_fullStr | Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry |
title_full_unstemmed | Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry |
title_short | Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry |
title_sort | folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2365927/ https://www.ncbi.nlm.nih.gov/pubmed/18394161 http://dx.doi.org/10.1186/1475-2859-7-12 |
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