title: Complete shift of ferritin oligomerization toward nanocage assembly via engineered protein-protein interactions.
abstract: Computational redesign of a dimorphic protein nano-cage at the C3-symmetrical interfaces forces it to assemble into the monomorphic cage. These monodisperse assemblies are at least 20 °C more stable than the parent. This approach adds to the toolkit of bottom-up molecular design with applications in protein engineering and hybrid nano-materials.
authors.affiliation: Department of Chemistry, School of Biomedical Sciences, King's College London, London, UK SE1 1UL.
authors.forename: Maziar S
authors.initials: MS
authors.lastname: Ardejani
authors.forename: Xiao Ling
authors.initials: XL
authors.lastname: Chok
authors.forename: Ce Jin
authors.initials: CJ
authors.lastname: Foo
authors.forename: Brendan P
authors.initials: BP
authors.lastname: Orner
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003573:Cytochrome b Group / Q000737:chemistry* / Q000235:genetics; D005293:Ferritins / Q000737:chemistry* / Q000235:genetics; D009154:Mutation; D049329:Nanostructures / Q000737:chemistry*; D011487:Protein Conformation; D015202:Protein Engineering
chemical_list: D001426:Bacterial Proteins; D003573:Cytochrome b Group; D005293:Ferritins; C018032:bacterioferritin