ABSTRACT
Two scientific developments that occurred in the early 1990s brought to the fore a new approach to solving biomolecular structures and enabled scientists in a wide variety of fields to make great strides in solving biological and pathophysiological problems. The first breakthrough was the completion of the Human Genome Project, which identified all the approximately 25,000 genes in human DNA and determined the sequences of the 3 billion chemical base pairs that make up human DNA, which were then translated into the proteins they code for and stored in huge databases that were made available to all scientists.(1-3) The other breakthrough was the development of two new mass spectrometric techniques: matrix-assisted laser desorption/ ionization (MALDI) and electrospray ionization (ESI). The mass spectrometers were user friendly yet high performance, thus by combining these advances the scientific community was able to identify and characterize a wide variety of biomolecules, often from as little as a few femtomoles.(2,3) However, as technical progress is always on the march, one of the latest and most exciting breakthroughs was the coupling of ion mobility (IM) and mass spectrometry (MS),(4-6) as structure elucidation is an arduous task with a constant need for improved instrumentation and methodology in order to study lipids and proteins that are present in trace amounts, which is often the case for nonstructural proteins as cells are the most efficient entities in existence, thus proteins are only manufactured when needed.
