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- W2026698321 abstract "Many spherical viruses assemble their capsids around their nucleic acid, a reaction that may involve hundreds of individual molecules. Yet, uniform virus-like particles appear to assemble quickly. To dissect the assembly mechanism and genome encapsidation, we have established a simplest case experimental system. We show that mixing SV40 VP1 pentamers with RNA 500 mers yields T=1 particles comprised of 12 pentamers and one RNA molecule. We examined the kinetics of this reaction by Time-Resolved Small Angle X-ray Scattering (TR-SAXS). TR-SAXS shows that assembly is very fast; the reaction is nearly third-complete at 35 ms when mixing 0.5 μM RNA and 7.5 μM VP1 pentamers. Nonetheless, assembly appears to be a two-state process with only free pentamers and capsids observed; intermediates are undetectable. Finally, we show that TR-SAXS data are very well fit by master equations that describe assembly as a nucleation of an RNA molecule with one, two or three pentamers, followed by a cascade of elongation reactions in which one pentamer is added at a time. From this model, we estimate that the molar rate constant for addition of pentamers is approximately 109 M−1 s−1. Such a rate is possible only if facilitated by long-ranged distance protein-nucleic acid attraction. We therefore suggest that the growing nucleo-protein complex is able to act as an electrostatic antenna for attracting other capsid subunits." @default.
- W2026698321 created "2016-06-24" @default.
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- W2026698321 date "2012-01-01" @default.
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- W2026698321 title "High Resolution Time-Resolved SAXS shows that RNA-Induced SV40 Capsid Protein Self-Assembly is very Fast and without Detectable Concentrations of Intermediates" @default.
- W2026698321 doi "https://doi.org/10.1016/j.bpj.2011.11.3501" @default.
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