Conformational Dynamics and Interactions of Membrane Proteins by Hydrogen/Deuterium Mass Spectrometry
Methods in molecular biology (Clifton, N.J.).
2016 ;
1432 () :
269-79.
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
Persistent link
https://www.medvik.cz/link/pmid27485342
- Keywords
- Conformational change, Dynamics, Hydrogen/deuterium exchange, Interaction, Mass spectrometry, Membrane protein,
- MeSH
- Mass Spectrometry instrumentation methods MeSH
- Protein Conformation MeSH
- Membrane Proteins chemistry metabolism MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Deuterium Exchange Measurement instrumentation methods MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Membrane Proteins MeSH
Hydrogen/deuterium exchange associated with mass spectrometry has been recently used to characterize the dynamics and the interactions of membrane proteins. Here we describe experimental workflow enabling localization of the regions involved in conformational changes or interactions.
BioCeV Institute of Microbiology Czech Academy of Sciences Vestec Czech Republic
Faculty of Science Charles University Prague Prague Czech Republic
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