[Physico-chemical characteristics of ribosomal proteins L10 and L11]

Abstract

The procedure of isolation and purification of ribosomal proteins L10 and L11 from the 50S subparticle of E. coli ribosomes is described. Sedimentation data, spectra of circular dichroism and the results of microcalorimetric studies are given for these proteins. It has been shown that in the range of the concentrations studied protein L11 does not associate in solution. Protein L10 has a tendency to self-association at increased concentrations (over 1.5 mg/ml). Protein L10 also forms a complex with the intact ribosomal protein L7. From the data presented it follows that protein L7 binds to protein L10 in a dimer form and the regions of L7 responsible for its dimerization participate in binding. It has been also shown that the proteins in solution have a rather low thermostability. An assumption is made on the stabilization of proteins within the ribosomes or in the complex with other ribosomal proteins.