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

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

doi:10.1021/ja066329n

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

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

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

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.

Original language	English
Pages (from-to)	15970-15971
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	128
Issue number	50
DOIs	https://doi.org/10.1021/ja066329n
State	Published - 20 Dec 2006
Externally published	Yes

Funding

Funders	Funder number
National Institute of General Medical Sciences	R01GM058914
National Institute of Biomedical Imaging and Bioengineering	R01EB003152

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10.1021/ja066329n

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title = "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.",

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AU - Miller, Paul A.

AU - Shajani, Zahra

AU - Meints, Gary A.

AU - Caplow, Dorothy

AU - Goobes, Gil

AU - Varani, Gabriele

AU - Drobny, Gary P.

PY - 2006/12/20

Y1 - 2006/12/20

N2 - 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.

AB - 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.

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

Abstract

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