Structure of Ribosomal Protein L6 from Escherichia coli
作者： Klaus G. STEINHÄUSER , Paul WOOLLEY , Bernd EPE , Jan DIJK
DOI: 10.1111/J.1432-1033.1982.TB06913.X
关键词: Chemistry 、 Ribosomal RNA 、 Quenching (fluorescence) 、 Ribosomal protein 、 Crystallography 、 Fluorophore 、 Ribosome 、 Acceptor 、 Fluorescence 、 Protein subunit
摘要: Protein L6 from the 50-S ribosomal subunit has been investigated using fluorimetric techniques. The intrinsic fluorophore Trp-61 and fluorescent labels (acetylaminoethyl-dansyl acetylaminofluorescein) attached to residue Cys-124 were used. It proved possible incorporate fluorescence-labelled into ribosome. Trp-61 is exposed solvent, as shown by its emission wavelength quenching experiments; latter also show that it lies in a pocket with high positive charge due basic residues N-terminal fragment. less strongly region. Upon incorporation subunit, label on becomes accessible for but potential rises, showing absence of direct contact 23-S RNA. Analysis anisotropy data indicates considerable degree asphericity free L6. Energy transfer between dansyl Cys-124, measured donor acceptor enhancement, reveals separation 3.5 ± 0.4 nm (35 4A) fluorophores.
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