title: Contrasting views of the internal dynamics of the HhaI 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-mus motions contribute to the functionally relevant dynamic properties of nucleic acids during DNA methylation.
authors.affiliation: Department of Chemistry, University of Washington, Seattle, Washington 98195, USA.
authors.forename: Paul A
authors.initials: PA
authors.lastname: Miller
authors.forename: Zahra
authors.initials: Z
authors.lastname: Shajani
authors.forename: Gary A
authors.initials: GA
authors.lastname: Meints
authors.forename: Dorothy
authors.initials: D
authors.lastname: Caplow
authors.forename: Gil
authors.initials: G
authors.lastname: Goobes
authors.forename: Gabriele
authors.initials: G
authors.lastname: Varani
authors.forename: Gary P
authors.initials: GP
authors.lastname: Drobny
mesh_terms: D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D015257:DNA-Cytosine Methylases / Q000737:chemistry* / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy
chemical_list: D004247:DNA; C037664:DNA modification methylase HhaI; D015257:DNA-Cytosine Methylases