Self-assembly can govern higher order protein structure, and protein-protein interactions are fundamental to this assembly.   By the use of domain swapping, alanine shaving, and computer-based design, we investigate the role of protein-protein interactions in the formation of hollow, nano-scaled ferritin cage proteins.  These mutagenesis studies have resulted in the identification of key domains and residues that strongly influence the assembly and overall protein stability.  These studies have also provided insight into the general self-assembly process allowing us to rationally design cages with enhanced stability. Furthermore, we describe a novel and general two step reduction technique for the clean and homogeneous production of gold nano-particles and gold/silver mixed nano-particles inside unmodified nano-cage proteins.

Unraveling the structural energetics of self-assembling protein cages and their application to nanomaterials

243rd National Meeting (2012)

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