Mapping membrane protein palmitoylation by native mass spectrometry

Palmitoylation of membrane proteins can be monitored by native mass spectrometry. A report from the labs of Piet Gros and Albert Heck of Utrecht University in The Netherlands, published today in Nature Communications, shows how native MS can be utilized to understand the post-translational modification in membrane proteins. The team demonstrates that any cysteine within 8 Å of the membrane gets palmitoylated, without the requirement for a specific sequence motif. The findings shed light on the biochemical requirements for membrane protein palmitoylation and could be of particular interest to protein design and engineering.

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