Publication | Closed Access
A Robust, Detergent-Friendly Method for Mass Spectrometric Analysis of Integral Membrane Proteins
165
Citations
24
References
2000
Year
X-ray CrystallographyProteinlipid InteractionMolecular BiologyIntegral Membrane ProteinsMembrane ProteinsProtein PurificationProtein FoldingBioanalysisStructure DeterminationProtein X-ray CrystallographyProteomicsMass Spectrometric AnalysisBiophysicsBiochemistryIon ChannelsMembrane BiologyDetergent-friendly MethodComputational Mass SpectrometryCrystallographyStructural BiologyNatural SciencesMass SpectrometryProtein Mass SpectrometryMedicine
Recent breakthroughs in the high-resolution structural elucidation of ion channels and transporters are prompting a growing interest in methods for characterizing integral membrane proteins. These methods are proving extremely valuable in facilitating the production of X-ray diffraction-grade crystals. Here we present a robust and straightforward mass spectrometric procedure that utilizes matrix-assisted laser desorption/ionization to analyze integral membrane proteins in the presence of detergents. The utility of this method is illustrated with examples of high-quality mass spectral data obtained from membrane proteins for which atomic resolution structural studies are ongoing.
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