This monograph reviews all relevant technologies based on mass spectrometry that are used to study or screen biological interactions in general.
Arranged in three parts, the text begins by reviewing techniques nowadays almost considered classical, such as affinity chromatography and ultrafiltration, as well as the latest techniques. The second part focusses on all MS-based methods for the study of interactions of proteins with all classes of biomolecules. Besides pull down-based approaches, this section also emphasizes the use of ion mobility MS, capture-compound approaches, chemical proteomics and interactomics. The third and final part discusses other important technologies frequently employed in interaction studies, such as biosensors and microarrays.
For pharmaceutical, analytical, protein, environmental and biochemists, as well as those working in pharmaceutical and analytical laboratories.
This monograph reviews all relevant technologies based on mass spectrometry that are used to study or screen biological interactions in general. Different distinct areas for analysis of bioaffinity interactions can be recognized in this regard. These areas include pre-column based ligand trapping followed by MS analysis, affinity chromatography following MS and post column on-line affinity profiling. Other methodologies relate to separately performed bioassays and (LC) MS analysis. Besides these, direct approaches are nowadays also used in several research areas and include direct MS based bioassays and native MS studies in which the latter looks at intact protein complexes in the gas phase.