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

Methods Mol Biol. 2016;1432:269-79. doi: 10.1007/978-1-4939-3637-3_17.

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.

Keywords: Conformational change; Dynamics; Hydrogen/deuterium exchange; Interaction; Mass spectrometry; Membrane protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Deuterium Exchange Measurement / instrumentation*
  • Deuterium Exchange Measurement / methods
  • Mass Spectrometry / instrumentation
  • Mass Spectrometry / methods
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism*
  • Protein Binding
  • Protein Conformation

Substances

  • Membrane Proteins