Secondary structure prediction of plant virus coat proteins.

Application of the secondary structure prediction techniques to the coat protein amino acid sequences of turnip yellow mosaic virus and satellite tobacco necrosis virus yielded an excellent correlation with the patterns of secondary structural elements observed in the capsid proteins of southern bean mosaic virus and tomato bushy stunt virus. Helical predictions for the very basic N-terminal regions of three plant viruses suggested modes of protein-nucleic acid interaction similar to those proposed for histones and protamines.