TOP 3
Ion Activation, Unfolding, and Dissociation Strategies for Native Proteomics and Protein Quaternary Structure Discovery — Leads: Brandon Ruotolo and Steffen Lindert
TOP 3 develops collision- and surface-induced unfolding to screen biomolecular stability, adapts technologies for vendor-specific complex down/native-omics approaches, and constructs integrated computations that utilize synergistic MS restraints to predict protein quaternary structures. TOP3 combines existing vendor technology with the TOP1 and TOP2 developments, while also providing stability testing with collision-induced and surface-induced unfolding (CIU/SIU) and unique activation combinations (e.g., ECD-SID and SID-ECD as compact devices to allow native-omics studies).
Aim 1
SIU/CIU methodologies for improved biomolecular fingerprinting and rapid stability assessments.
Aim 2
Ion activation techniques for native proteomics and proteoform identification.
Aim 3
Integrated modeling approaches for the construction of protein quaternary structure models based on MS data.