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Counterion Release Stabilizes Multi-Shell Structures Of Virus Coat Proteins

TitleCounterion Release Stabilizes Multi-Shell Structures Of Virus Coat Proteins
Publication TypeJournal Article
Year of Publication2009
AuthorsPrinsen, P, van der Schoot, P, Gelbart, WM, Knobler, CM
JournalBiophysical Journal
Volume96
Pagination422a
Abstract

Under conditions of low ionic strength and a pH between about 3.5 and 5.0, solutions of purified coat proteins of cowpea chlorotic mottle virus (CCMV) form spherical multi-shell structures in the absence of viral RNA. The native protein shell, which has an outer diameter of about 28 nm and is built up from 180 coat proteins, forms the inner shell and is surrounded by one or two larger concentric shells. We show that counterion release is the main force stabilizing these multi-shell structures, arguing that this compensates for the outer shells not being able to adopt their smaller optimal radius of curvature.

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