Constructing protein polyhedra via orthogonal chemical interactions.

ABSTRACT: Many proteins exist naturally as symmetrical homooligomers or homopolymers¹. The emergent structural and functional properties of such protein assemblies have inspired extensive efforts in biomolecular design^2-5. As synthesized by ribosomes, proteins are inherently asymmetric. Thus, they must acquire multiple surface patches that selectively associate to generate the different symmetry elements needed to form higher-order architectures^1,6-a daunting task for protein design. Here we address this problem using an inorganic chemical approach, whereby multiple modes of protein-protein interactions and symmetry are simultaneously achieved by selective, 'one-pot' coordination of soft and hard metal ions. We show that a monomeric protein (protomer) appropriately m

SUBMITTER: Golub E 

PROVIDER: S-EPMC7007351 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature