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1. Contrasting views of the internal dynamics of the HhaI methyltransferase target DNA reported by solution and solid-state NMR spectroscopy

Author

Miller, Paul A., Shajani, Zahra, Meints, Gary A., Caplow, Dorothy, Goobes, Gil, Varani, Gabriele, and Drobny, Gary P.

Subjects
Nuclear magnetic resonance spectroscopy -- Usage, Methylation -- Observations, Molecular dynamics -- Research, Chemistry
Abstract

Solid state and solution NMR are used to investigate internal motions at six positions near the HhaI methyltransferase enzyme recognition site for the [[5'-(dGATAGCGCTATC)-3'].sub.2] DNA dodecamer. The results have shown that the HhaI DNA methylation target site possesses an intrinsically dynamic structure and the measurements of dynamics for many nucleotides in the vicinity of the methylation site have identified two residues that experience significant mobility in the absence of the methylase.

Published
2006

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