Complete shift of ferritin oligomerization toward nanocage assembly via engineered protein-protein interactions

Maziar S. Ardejani; Xiao Ling Chok; Ce Jin Foo; Brendan P. Orner

doi:10.1039/c3cc40886h

Complete shift of ferritin oligomerization toward nanocage assembly via engineered protein-protein interactions

Maziar S. Ardejani, Xiao Ling Chok, Ce Jin Foo, Brendan P. Orner^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

32 Citations (Scopus)

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.

Original language	English
Pages (from-to)	3528-3530
Number of pages	3
Journal	CHEMICAL COMMUNICATIONS- ROYAL SOCIETY OF CHEMISTRY
Volume	49
Issue number	34
DOIs	https://doi.org/10.1039/c3cc40886h
Publication status	Published - 4 May 2013

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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.",

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AU - Orner, Brendan P.

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AB - 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.

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Complete shift of ferritin oligomerization toward nanocage assembly via engineered protein-protein interactions

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