Article
Folding mechanism of the Tetrahymena ribozyme P4-P6 domain.
Biochemistry - 12 Sept 2000
Deras M L, Brenowitz M, Ralston C Y, Chance M R, Woodson S A
Abstract excerpt
Synchrotron X-ray-dependent hydroxyl radical footprinting was used to probe the folding kinetics of the P4-P6 domain of the Tetrahymena group I ribozyme, which forms a stable, closely packed tertiary structure. The 160-nt domain folds independently at a similar rate (approximately 2 s(-1)) as it does in the ribozyme, when folding is measured in 10 mM sodium cacodylate and 10 mM MgCl(2). Surprisingly, tertiary...
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