Journal
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
Volume 30, Issue 1, Pages 181-191Publisher
SPRINGER
DOI: 10.1007/s13361-018-2061-4
Keywords
Native mass spectrometry; LILBID; nESI; Soluble proteins; Membrane proteins; Ion source
Funding
- DFG (German Research Foundation), Collaborative Research Center 807 Transport and Communication across Biological Membranes
- state of Hessen/Center for Biomolecular Magnetic Resonance (BMRZ)
- Cluster of Excellence Frankfurt (Macromolecular Complexes)
- European Research Council under the European Union's Seventh Framework Programme (FP7/2007-2013) / ERC Grant [337567]
- European Research Council (ERC) [337567] Funding Source: European Research Council (ERC)
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Native mass spectrometry is applied for the investigation of proteins and protein complexes worldwide. The challenge in native mass spectrometry is maintaining the features of the proteins of interest, such as oligomeric state, bound ligands, or the conformation of the protein complex, during transfer from solution to gas phase. This is an essential prerequisite to allow conclusions about the solution state protein complex, based on the gas phase measurements. Therefore, soft ionization techniques are required. Widely used for the analysis of protein complexes are nanoelectro spray ionization (nESI) mass spectrometers. A newer ionization method is laser induced liquid bead ion desorption (LILBID), which is based on the release of protein complexes from solution phase via infrared (IR) laser desorption. We use both methods in our lab, depending on the requirements of the biological system we are interested in. Here we benchmark the performance of our LILBID mass spectrometer in comparison to a nESI instrument, regarding sample conditions, buffer and additive tolerances, dissociation mechanism and applicability towards soluble and membrane protein complexes.
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