Andrew Alpert | Authors


Preview of Topics at HPLC 2016, III: Reconsidering HIC for Top-Down Proteomics

Until recently, mass spectrometry (MS) was limited in the information it could supply regarding proteins larger than 40 kDa. The most recent instruments have broken through that limit, but proteins smaller than 40 kDa are still more easily detected in MS and can suppress the collection of data from larger proteins. This situation has created a demand for better separation of proteins upstream from the MS orifice. At present, though, this separation of proteins is something of a bottleneck. Methods such as reversed-phase chromatography that involve mobile phases compatible with MS are not compatible with many proteins. Alternative modes of chromatography include size-exclusion chromatography, ion-exchange chromatography, hydrophilic interaction chromatography (HILIC), and hydrophobic interaction chromatography (HIC). We decided to take another look at HIC. This is the third in a series of articles exploring topics that will be addressed at the HPLC 2016 conference in San Francisco, from June 19 to 24.