title: Conformational changes in 16S ribosomal RNA induced by 30S ribosomal subunit proteins from Escherichia coli.
abstract: Laser light scattering has been used to evaluate conformational differences between free 16S RNA and several specific protein-16S RNA complexes. Proteins that interact strongly with the 16S RNA early in subunit assembly stabilize the RNA chain against unfolding in 1 mM Mg2+ and actually promote the formation of a more compact teriary structure in 20 mM Mg2+. A vital function of these proteins may therfore consist in altering the configuration of the RNA so that further assembly reactions can take place.
mesh_terms: D001426:Bacterial Proteins; D004058:Diffusion; D004926:Escherichia coli; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D012329:RNA, Bacterial; D012335:RNA, Ribosomal; D012261:Ribonucleoproteins; D012269:Ribosomal Proteins; D012270:Ribosomes / Q000648:ultrastructure*
chemical_list: D001426:Bacterial Proteins; D012329:RNA, Bacterial; D012335:RNA, Ribosomal; D012261:Ribonucleoproteins; D012269:Ribosomal Proteins