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

Abstract

Solution and solid-state NMR have been used conjointly to probe the internal motions of a DNA dodecamer containing the recognition site for the HhaI methyltransferase. The results strongly suggest that ns-μs motions contribute to the functionally relevant dynamic properties of nucleic acids during DNA methylation.

Department(s)

Chemistry and Biochemistry

Document Type

Article

DOI

https://doi.org/10.1021/ja066329n

Publication Date

12-20-2006

Journal Title

Journal of the American Chemical Society

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