Transient membrane protein complexes require advanced biochemical approaches to stabilize the dynamic fluctuations in their composition and prevent dissociation during sample preparation. Stabilized complexes can be subject to multi-facetted analysis to relate changes in their architecture to changes in their composition and thereby follow their dynamic behavior. Current structural studies of membrane proteins and complexes have focused on stably pre-assembled macromolecules.
RA3 is designed to provide insights into dynamic PPIs and how membrane proteins interact with transient or weak interacting factors. Unstable, macromolecular membrane protein assemblies have so-far escaped full characterization due to a lack of suitable methods; our developed approaches will be of major importance to others working with instable membrane protein complexes.