Mass spectrometry for protein structure studies – selected applications
Michał Dadlez, Laboratory of Mass Spectrometry, Institute of Biochemistry and Biophysics, Polish Academy of Sciences (IBB-PAS), Warsaw, Poland
The application of mass spectrometry for protein studies extends far beyond classic proteomic analyses in which proteins and their posttranslational modifications are identified and/or quantified.
Recent developments of new approaches, like ion mobility separation (providing access to collisional cross section values) or technical improvements in the methods already known (like measurements of the hydrogen-deuterium exchange kinetics) enable efficient application of mass spectrometry for protein structure studies.
Using these methods new experimental constraints can be obtained for protein assemblies (like natively unstructured proteins, membrane or aggregating proteins) which for some reason cannot be analyzed by classic structural methods like crystallography or NMR. Short introduction to these new approaches will be presented followed by a few examples of their application.
Ion mobility measurements brought new information on the structures of Abeta peptide (Alzheimer’s disease peptide) oligomers. HDex was applied in numerous projects on protein structure, oligomerization, heterocomplex interface mapping and protein lipid interactions.
