AlphaFold can be used to predict the oligomeric states of proteins

Homooligomerisation is a prevalent and important process that many proteins undergo to form the quaternary structure required to carry out their biological functions. However, determining the oligomeric states and structures of some proteins through experimental methods remains technically challenging and time consuming. Here, we show that the protein structure prediction tools AlphaFold2-Multimer and AlphaFold3 can be used to quickly and accurately predict the oligomeric states and structures of soluble and membrane proteins. We provide optimal parameters for minimizing computational cost while maintaining accuracy, apply this technique to several membrane proteins of interest, and highlight instances where multiple physiologically relevant oligomeric states of a given protein can be predicted using this method.