title: Chemical modifications of DNA for study of helicase mechanisms.
abstract: Helicases are ubiquitous enzymes that are required for virtually all processes in DNA and RNA metabolism including replication, repair, recombination, transcription, and translation. The mechanisms for helicase-catalyzed unwinding of double-stranded DNA or remodeling of RNA have been the subject of intense investigation for more than two decades. The central function of these enzymes is to transduce the energy available from ATP binding and hydrolysis to alter the conformation of nucleic acids. Specific interactions between helicases and nucleic acids have been investigated by chemical approaches in which the nucleic acid substrate has been modified in order to provide specific insight into the enzymatic mechanism.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, 4301 W. Markham St., Slot 516, Little Rock, AR 72205, USA. Electronic address: raneykevind@uams.edu.
authors.forename: Kevin D
authors.initials: KD
authors.lastname: Raney
mesh_terms: D055162:Biocatalysis; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D004265:DNA Helicases / Q000378:metabolism*
chemical_list: D004247:DNA; D004265:DNA Helicases
keywords: Abasic site; Biotinylated DNA; DNA unwinding; FRET; Methylphosphonate; Peptide nucleic acid