LILBID and nESI: Different Native Mass Spectrometry Techniques as Tools in Structural Biology
Autor: | Nils Hellwig, Erik Henrich, Oliver Peetz, Volker Dötsch, Frank Bernhard, Julija Mezhyrova, Nina Morgner |
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Jazyk: | angličtina |
Rok vydání: | 2018 |
Předmět: |
Soluble proteins
Chemistry 010401 analytical chemistry Analytical chemistry 010402 general chemistry Proteomics Mass spectrometry 01 natural sciences Dissociation (chemistry) Ion source 0104 chemical sciences Ion Native mass spectrometry Structural biology nESI Structural Biology Desorption Ionization ddc:570 ddc:540 Membrane proteins LILBID Focus: Honoring Carol V. Robinson's Election to the National Academy of Sciences: Research Article Spectroscopy |
Zdroj: | Journal of the American Society for Mass Spectrometry |
ISSN: | 1879-1123 1044-0305 |
Popis: | 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. Graphical Abstractᅟ Electronic supplementary material The online version of this article (10.1007/s13361-018-2061-4) contains supplementary material, which is available to authorized users. |
Databáze: | OpenAIRE |
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