The need for conformational information is increasing by the time in studies
on macromolecules. For example, proteins may have various functions and properties
depending on their folding states that make their conformational analyses very
important. Mass spectrometry is one of the most effective analytical techniques that
separate ions in the gas phase by their mass-to-charge ratio. It provides useful data on
molecular characterization in many areas of research with high precision, accuracy, and
sensitivity. Although mass spectrometry is a very powerful analytical technique, it
cannot distinguish different species having identical mass-to-charge ratio. The
analytical technique combining mass spectrometry with ion mobility spectrometry
(IM-MS), which provides information about the three-dimensional structure of an ion,
solves this problem by separating them according to their collision cross sections
(CCS) in the gas phase. This analytical method also provides the advantages of higher
precision and better resolution in the rapid analysis of different types of complex
samples. The separation of isomers with the same molecular weight, increasing the
dynamic range and distinguishing ions from chemical noise are the most important
features that this technique contributes to mass spectrometry. As improvements have
been made in IM-MS technology, the number and quality of publications in the areas
where this technique is used increases rapidly. In this chapter, the use of IM-MS
techniques in the fields such as proteomics, glycoproteomics and polymer
characterization are explained by presenting their various applications in the literature.
Keywords: Conformational Characterization, Glycoproteomics, Ion Mobility-Mass Spectrometry, Proteomics, Polymer Characterization.
