dc.contributor.authorPeng, Tao
dc.contributor.authorLee, Hwankyu
dc.contributor.authorLim, Sierin
dc.date.accessioned2013-08-01T03:51:08Z
dc.date.available2013-08-01T03:51:08Z
dc.date.copyright2012en_US
dc.date.issued2012
dc.identifier.citationPeng, T., Lee, H.,& Lim, S. (2012). Isolating a Trimer Intermediate in the Self-Assembly of E2 Protein Cage. Biomacromolecules, 13(3), 699-705.en_US
dc.identifier.urihttp://hdl.handle.net/10220/12755
dc.description.abstractUnderstanding the self-assembly mechanism of caged proteins provides clues to develop their potential applications in nanotechnology, such as a nanoscale drug delivery system. The E2 protein from Bacillus stearothermophilus, with a virus-like caged structure, has drawn much attention for its potential application as a nanocapsule. To investigate its self-assembly process from subunits to a spherical protein cage, we truncate the C-terminus of the E2 subunit. The redesigned protein subunit shows dynamic transition between monomer and trimer, but not the integrate 60-mer. The results indicate the role of the trimer as the intermediate and building block during the self-assembly of the E2 protein cage. In combination with the molecular dynamics simulations results, we conclude that the C-terminus modulates the self-assembly of the E2 protein cage from trimer to 60-mer. This investigation elucidates the role of the intersubunit interactions in engineering other functionalities in other caged structure proteins.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesBiomacromoleculesen_US
dc.titleIsolating a trimer intermediate in the self-assembly of E2 protein cageen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Chemical and Biomedical Engineeringen_US
dc.identifier.doihttp://dx.doi.org/10.1021/bm201587q


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