Complete shift of ferritin oligomerization toward nanocage assembly via engineered protein-protein interactions
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...
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Published in | Chemical communications (Cambridge, England) Vol. 49; no. 34; pp. 3528 - 3530 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
England
01.01.2013
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Subjects | |
Online Access | Get full text |
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Summary: | 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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1359-7345 1364-548X |
DOI: | 10.1039/c3cc40886h |