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  LILBID based assessment of binding affinities

The association and dissociation of non-covalently interacting species play a vital role in various biological processes, ranging from the formation of DNA double helices to the functional interplay of subunits in molecular machines. To study the pathways of these reactions, it is crucial to not only determine the interacting partners and their stoichiometry, but to further characterize their interactions in terms of binding affinities.
With the possibility to detect biomolecules and their non-covalently bound complexes via LILBID-MS, the subsequent objective is therefore to gain information about the molar quantities of bound and unbound species in solution. However, peak areas in the mass spectra are not directly correlated to the concentration of respective species in their native environment due to various factors, such as dissociation of bonds during desorption in the ion source or varying ionization efficiencies of different species. Therefore, this project aims to identify and account for these factors to enable the determination of quantitative values such as the dissociation constant of specific interactions.