[Secondary structure of total protein and 23S RNA in 50S ribosomal subunits and in the isolated state].
Optical and sedimentational studies of isolated 23S RNA, total proteins and some RNP-complexes of the 50S subunits were carried out. It is shown that the secondary structure content of 23S RNA in the ribosome is lower than in the isolated state. Ribosomal proteins stabilize the 23S RNA structure and make it more compact. At the same time they cause some unwinding effect on the secondary structure of the 23S RNA and possibly fix some segments of the 23S RNA in the conformation necessary for its function. In turn, the 23S RNA increased somewhat the level of the total ordered secondary structure in the ribosomal proteins. There was no considerable change of the ratio between the alpha- and beta-structures in the proteins.
G M
GM
Gongadze
A T
AT
Gudkov
S Iu
SIu
Ven'iaminov
D001426:Bacterial Proteins / Q000032:analysis; D002942:Circular Dichroism; D004926:Escherichia coli / Q000032:analysis; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D012329:RNA, Bacterial / Q000032:analysis; D012335:RNA, Ribosomal / Q000032:analysis*; D012269:Ribosomal Proteins / Q000032:analysis*; D012270:Ribosomes / Q000032:analysis*; D013056:Spectrophotometry, Ultraviolet
D001426:Bacterial Proteins; D012329:RNA, Bacterial; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins
Vtorichnaia struktura summarnogo belka i 23S RNK v sostave 50S subchastits i v izolirovannom vide.