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Ion mobility–mass spectrometry as a tool to investigate protein–ligand interactions

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons104330

Göth,  Melanie
Institute of Chemistry and Biochemistry, Freie Universität Berlin;
Molecular Physics, Fritz Haber Institute, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons32738

Pagel,  Kevin
Institute of Chemistry and Biochemistry, Freie Universität Berlin;
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Citation

Göth, M., & Pagel, K. (2017). Ion mobility–mass spectrometry as a tool to investigate protein–ligand interactions. Analytical and Bioanalytical Chemistry. doi:10.1007/s00216-017-0384-9.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-7191-5
Abstract
Ion mobility–mass spectrometry (IM-MS) is a powerful tool for the simultaneous analysis of mass, charge, size, and shape of ionic species. It allows the characterization of even low-abundant species in complex samples and is therefore particularly suitable for the analysis of proteins and their assemblies. In the last few years even complex and intractable species have been investigated successfully with IM-MS and the number of publications in this field is steadily growing. This trend article highlights recent advances in which IM-MS was used to study protein–ligand complexes and in particular focuses on the catch and release (CaR) strategy and collision-induced unfolding (CIU).