Abstract

Proteins are highly dynamic entities. Their myriad functions require specific structures, but proteins’ dynamic nature ranges all the way from the local mobility of their amino acid constituents to mobility within and well beyond single cells.

A truly comprehensive view of the dynamic structural proteome includes: (1) alternative sequences, (2) alternative conformations, (3) alternative interactions with a range of biomolecules, (4) cellular localisations, (5) alternative behaviours in different cell types. While these aspects have traditionally been explored one protein at a time, we explore recently emerging global approaches that accelerate comprehensive insights into these facets of the dynamic nature of protein structure.

We use chemical crosslinking with a gas-phase cleavable linker and enzymatic biotin-labeling to gain complementary insights into protein complexes and cellular architectures