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Conformational Dynamics and Interactions of Membrane Proteins by Hydrogen/Deuterium Mass Spectrometry

  • Eric Forest
  • Petr Man
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 1432)

Abstract

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.

Key words

Hydrogen/deuterium exchange Mass spectrometry Conformational change Dynamics Interaction Membrane protein 

Notes

Acknowledgements

PM acknowledges, LQ1604 NPU II provided by MEYS and CZ.1.05/1.1.00/02.0109 BIOCEV provided by ERDF and MEYS and grant from Charles University in Prague (GAUK 389115).

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Copyright information

© Springer Science+Business Media New York 2016

Authors and Affiliations

  1. 1.Univ. Grenoble Alpes, IBSGrenobleFrance
  2. 2.CNRS, IBSGrenobleFrance
  3. 3.CEA, IBSGrenobleFrance
  4. 4.Institut de Biologie Structurale, CNRS (UMR 5075)/CEA/UGAGrenoble Cedex 9France
  5. 5.BioCeV - Institute of MicrobiologyCzech Academy of SciencesVestecCzech Republic
  6. 6.Faculty of ScienceCharles University in PraguePragueCzech Republic

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