Low-dimensional quantum materials are under considerable investigation for exploiting their unique properties within functional devices. While these materials have been extensively studied for their properties and applications, notable gaps in terms of their thermal stability and behavior remain, particularly with respect to typical device fabrication temperatures.

Lead halide perovskite nanocrystal (PNC) materials have garnered much attention lately because of their fascinating optical and optoelectronic characteristics. These characteristics make them excellent candidates for photovoltaic applications with high power conversion efficiencies for solar cell applications. However, degradation during thermal treatment and poor stability against moisture and UV light are common problems for PNCs.

N-linked glycosylation is an important post translational modification, and the changes in N-glycan patterns are known to be associated with various human diseases. The study of N-glycans is crucial for the safety and efficacy of biotherapeutics. Tandem mass spectrometry (MS/MS) is a popular method in glycomics where glycans are identified via their mass to charge (m/z) and fragment ions. However, glycans exist as isomers arising from linkage, anomeric, and stereochemical differences.

Ion mobility spectrometry-mass spectrometry has emerged as an orthogonal and complementary analytical technique to liquid chromatography-tandem mass spectrometry in omics-based analyses. Carbohydrate-containing molecules, such as human milk oligosaccharides and glycolipids, are notoriously difficult to characterize, largely owing to their high degrees of isomeric heterogeneity. Thus, new analytical methodologies are required to improve the confidence of their characterization.

The sequencing of intact proteins within a mass spectrometer enables the profiling of post-translational modification (PTM) crosstalk but is frequently hindered by convoluted spectra and the fact that tandem mass spectrometry (MS/MS) techniques often generate poor sequence coverages when applied to protein ions. Ion mobility spectrometry is a promising tool to overcome the complexity of these spectra by separating ions by their mass- and size-to-charge ratios.

The fundamental building blocks of life consist of lipids, carbohydrates, proteins, and nucleic acids which are assembled from small repeating monomer subunits. Specifically monosaccharides are the precursors of carbohydrates and amino acids are the building blocks of proteins. These two monomers are chiral (except glycine) and can exist in multiple stereochemical forms making their characterization complex.