Partial deproteinization of ribosomal subunits by treatment with high concentrations of sodium chloride: physical and chemical characterization of protein depleted particles.

Sedimentation of E. coli ribosomal subunits through sucrose gradients containing high concentrations of NaCl (0.1 - 1.0 M) brings about removal of a specific fraction of their proteins. The alterations in the structural properties of the subunits caused by dissociation of these proteins are studied. They appear to be, at least partly the result of removal of constraints on RNA conformation imposed by the released proteins.