Structural and Functional Studies on Protein S20 from the 30-S Subunit of the Escherichia coli Ribosome
作者： Konstantinos PATERAKIS , Jennifer LITTLECHILD , Paul WOOLLEY
DOI: 10.1111/J.1432-1033.1983.TB07083.X
关键词:
摘要: Fragments resistant to proteolysis have been obtained from the ribosomal protein S20. They provide evidence for a structural domain stretching middle of its C terminus. With exception large fragment this lacking only 14 residues at N terminus, all fragments had lost their ability bind 16-S rRNA. The in 16-S-RNA complex was highly protected against enzymic digestion, indicating that entire is involved interaction with nucleic acid. Circular dichroism showed high α helix content (36%) intact and low (2%) fragment. Intrinsic fluorescence studies demonstrated single tyrosine residue S20 exposed solvent not complex. Irreversible thermal denaturation followed by found between 50°C 70°C.
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