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Circular dichroism studies show that the RNA of turnip rosette virus (TRosV), both within the particles and free in solution, has considerable base pairing. The protein of TRosV is characterized by a relatively high proportion of β-structure and low proportion of α-helix. Swelling of the virus particles by raising the pH and removing divalent cations causes slight changes in the conformation of the RNA and some changes in the protein conformation.
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