Abstract

Structural insights into protein complexes have had a broad impact on our understanding of biological function and evolution. We seek a comprehensive understanding of the general principles underlying quaternary structure organization in protein complexes by examining the fundamental steps by which protein complexes can assemble. We use both experimental and structure-based characterization of assembly pathways. Most assembly transitions can be classified into three basic types, which can then be used to exhaustively enumerate a large set of possible quaternary structure topologies, which enables a natural organization of protein complexes into a periodic table, with important implications for quaternary structure prediction, modeling and engineering.

In recent work, we focus on homomeric protein complexes, and use in vitro and in vivo systems to study co-translational assembly. This reveals features of protein sequence and the cellular environment that govern successful assembly of homomers. These are relevant to protein design and expression optimisation.