Contrasting views of the internal dynamics of the Hhal methyltransferase target DNA reported by solution and solid-state NMR spectroscopy
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.
Chemistry and Biochemistry
Miller, Paul A., Zahra Shajani, Gary A. Meints, Dorothy Caplow, Gil Goobes, Gabriele Varani, and Gary P. Drobny. "Contrasting Views of the Internal Dynamics of the Hh aI Methyltransferase Target DNA Reported by Solution and Solid-State NMR Spectroscopy." Journal of the American Chemical Society 128, no. 50 (2006): 15970-15971.
Journal of the American Chemical Society