Ultraviolet circular dichroism measurements on wheat embryo ribosomes and their constituent ribonucleates and proteins.

Circular dichroism measurements on wheat embryo ribosomes and their constituent RNA and proteins under conditions of physiological environment support the conclusion drawn from optical rotatory dispersion studies that the base-paired conformation of RNA in the ribosome is similar to that in the free state. Measurements on these systems in the virtual absence of salt suggest that the RNA in the ribosome maintains its double-helical character largely through stabilization interactions with the structural ribosomal proteins. In addition, no conformational change accompanies the dissociation of the 80 S ribosomal particle into its 40 and 26 S subunits.