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E L Christian et al.
Biochemistry, 37(50), 17618-17628 (1998-12-23)
The bacterial RNase P ribozyme is a site-specific endonuclease that catalyzes the removal of pre-tRNA leader sequences to form the 5' end of mature tRNA. While several specific interactions between enzyme and substrate that direct this process have been determined
S Basu et al.
Nature structural biology, 5(11), 986-992 (1998-11-10)
Metal ions are essential for the folding and activity of large catalytic RNAs. While divalent metal ions have been directly implicated in RNA tertiary structure formation, the role of monovalent ions has been largely unexplored. Here we report the first
Chun-Chi Wang et al.
Electrophoresis, 26(13), 2637-2642 (2005-06-04)
This study describes approaches for stacking a large volume of sample solutions containing a mixture of mercaptopurine monohydrate, 6-methylmercaptopurine, thioguanine, thioguanosine, and thioxanthine in capillary electrophoresis (CE). After filling the run buffer (60 mM borate buffer, pH 8.5), a large
I N Lavrik et al.
Molekuliarnaia biologiia, 38(5), 937-944 (2004-11-24)
Photoreactive derivatives of tRNAs, containing 6-thioguanosine or diazirine derivative of 5-methyleneaminouridine were compared as probes to modify Escherichia coli ribosomes. The derivatives of tRNA were synthesized by T7 transcription Proportion of the modified nucleotide analogues was optimised to obtain good
Alexandre de Lencastre et al.
Nature structural & molecular biology, 12(7), 626-627 (2005-06-28)
Despite the biological importance of self-splicing group II introns, little is known about their structural organization. Synthetic incorporation of site-specific photo-cross-linkers within catalytic domains resulted in functional distance constraints that, when combined with known tertiary interactions, provide a three-dimensional view
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