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Hydrophobic Interaction Chromatography for Bottom-Up Proteomics Analysis of Single Proteins and Protein Complexes

Hydrophobic interaction chromatography (HIC) is a robust standard analytical method to purify proteins while preserving their biological activity. It is widely used to study post-translational modifications of proteins and drug–protein interactions. In the current manuscript we employed HIC to separate proteins, followed by bottom-up LC–MS/MS experiments. We used this approach to fractionate antibody species followed by comprehensive peptide mapping as well as to study protein complexes in human cells. HIC–reversed-phase chromatography (RPC)–mass spectrometry (MS) is a powerful alternative to fractionate proteins for bottom-up proteomics experiments making use of their distinct hydrophobic properties.

Authors:   Michal Rackiewicz; Ludger Große-Hovest; Andrew J. Alpert; Mostafa Zarei; Jörn Dengjel
Journal:   Journal of Proteome Research
Year:   2017
DOI:   10.1021/acs.jproteome.7b00015
Publication date:   11-May-2017
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