Rackiewicz, Michal Große-Hovest, Ludger Alpert, Andrew J. Zarei, Mostafa Dengjel, Jörn 2017-06-02 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. application/pdf https://folia.unifr.ch/global/documents/305515 https://folia.unifr.ch/documents/305515/files/den_hic.pdf https://folia.unifr.ch/documents/305515/files/den_hic_sm.pdf eng info:eu-repo/semantics/altIdentifier/doi/10.1021/acs.jproteome.7b00015 info:eu-repo/semantics/openAccess License undefined Journal of Proteome Research. - 2017, vol. 16, no. 6, p. 2318–2323 info:eu-repo/classification/udc/57 Hydrophobic interaction chromatography for bottom-up proteomics analysis of single proteins and protein complexes http://purl.org/coar/resource_type/c_6501