Abstract
Structural features and thermodynamic parameters of the complete Chilo iridescent virus (Iridovirus type 6) and its constituents, isolated from the larvae of Galleria mellonella, were evaluated by means of UV spectroscopy and microcalorimetry. It can be demonstrated that the viral DNA is attached to the coat protein in a chromatin-like fashion, which is preserved after disruption of the virus by low temperature or partial digestion of the coat protein with proteinase K. At elevated temperature however the viral DNA is denaturated irreversibly. The coat protein appears to remain in its native state during the DNA transition and its own thermal denaturation profile shows its independence from the DNA denaturation.
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