Cells encode information in the sequence of biopolymers, such as nucleic acids, proteins,
and glycans. Although glycans are essential to all living organisms, surprisingly little is …

Trapped ion mobility spectrometry (TIMS) hybridized with mass spectrometry (MS) is a
relatively recent advance in the field of ion mobility mass spectrometry (IMMS). The basic …

Data-independent acquisition modes isolate and concurrently fragment populations of
different precursors by cycling through segments of a predefined precursor m/z range …

In bottom-up proteomics, peptides are separated by liquid chromatography with elution peak
widths in the range of seconds, whereas mass spectra are acquired in about 100 …

In liquid chromatography-mass spectrometry (LC-MS)-based proteomics, many precursors
elute from the column simultaneously. In data-dependent analyses, these precursors are …

Calculating the number of confidently identified proteins and estimating false discovery rate
(FDR) is a challenge when analyzing very large proteomic data sets such as entire human …

Recent advances in efficiency and ease of implementation have rekindled interest in ion
mobility spectrometry, a technique that separates gas phase ions by their size and shape …

Conspectus Native mass spectrometry is nowadays widely used for determining the mass of
intact proteins and their noncovalent biomolecular assemblies. While this technology …

Ion mobility can add a dimension to LC-MS based shotgun proteomics which has the
potential to boost proteome coverage, quantification accuracy and dynamic range. Required …

Ion mobility spectrometry is an analytical technique known for more than 100 years, which
entails separating ions in the gas phase based on their size, shape, and charge. While ion …