The major nucleocapsid protein of single nucleocapsid nuclear polyhedrosis virus is a low mol. wt., basic, DNA-binding protein present in the core of the capsid. It is rich in arginine and helix-destabilizing residues and possesses no lysine nor hydrophobic residues. Circular dichroism analysis showed that the protein undergoes a major conformational change in high salt solutions involving the tyrosine side chains. There is sufficient of this protein in the nucleocapsid for all the genome phosphate to be neutralized by arginine residues. A comparison of the protein with similar basic proteins from granulosis virus, non-occluded baculovirus, and multiple nucleocapsid nuclear polyhedrosis virus showed that they are all arginine-rich, lysine-poor, DNA-binding proteins.


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