Abstract

The strong tendency to aggregate of coat protein molecules of simple plant viruses has been represented by means of self-assembling molecular models. These models are made of ferrite magnets and are similar to molecular models designed for the purpose of simulating crystal structures. Capsid structures of isometric viruses are simulated by assembling dipolar spheres. The double-disk and helix structures of tobacco mosaic virus protein are simulated by assembling dipolar molecular models in a characteristic shape.

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