Abstract：
:Controlling self-assembly is critical to the advancement of nanotechnology. A rugged or crenated assembly energy surface can redirect assembly off path. By using a defined starting point and an energy surface made rough by a strong association energy, we can impose entirely new assembly paths and products. Normally, the coat protein (CP) of the Cowpea Chlorotic Mottle Virus (CCMV) assembles into virus-like 28 nm diameter icosahedral particles. Here we have started with the coat protein trapped in a rod-like structure in complex with DNA. When these 17 nm diameter rods are placed under the same condition, low pH, that normally leads to assembly of 28 nm diameter particles, we instead obtain 17 nm capsids. The extrusion of all-pentamer capsids from the hexagonal lattice of the rod demonstrates the importance of the starting state for controlled assembly.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Burns K,Mukherjee S,Keef T,Johnson JM,Zlotnick Adoi
10.1021/bm901160bsubject
Has Abstractpub_date
2010-02-08 00:00:00pages
439-42issue
2eissn
1525-7797issn
1526-4602journal_volume
11pub_type
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