Dr. John Young, a postdoctoral fellow in the Duong lab was interviewed by Science in the City this week regarding his recent publication in the Journal of Proteome Research.

In the research described in “His-Tagged Peptidiscs Enable Affinity Purification of the Membrane Proteome for Downstream Mass Spectrometry Analysis,” Dr. Young and colleagues employed His-tagged peptidiscs to enrich the reconstituted membrane proteome by affinity chromatography. Using mass spectrometry, they showed that the purified library sample is enriched in membrane proteins compared with the unpurified sample, and that ribosomal and other abundant soluble contaminants were strongly depleted. the researchers applied this method to survey global changes in the membrane proteome upon depletion of the SecDFyajC complex, an important ancillary subunit of the universally conserved Sec translocon. In this depleted strain, they detected increased membrane localization of the motor ATPase SecA, along with increased levels of an unannotated inner membrane protein, YibN.

These results demonstrate the utility of the peptidisc for global purification of membrane proteins and for monitoring changes in the membrane proteome.

Read more about Dr. Young, and the work underway in the laboratory of Dr. Franck Duong, Department of Biochemistry and Molecular Biology using peptidisc libraries in Science in the City‘s feature article.