title: Folding of a universal ribozyme: the ribonuclease P RNA.
abstract: Ribonuclease P is among the first ribozymes discovered, and is the only ubiquitously occurring ribozyme besides the ribosome. The bacterial RNase P RNA is catalytically active without its protein subunit and has been studied for over two decades as a model system for RNA catalysis, structure and folding. This review focuses on the thermodynamic, kinetic and structural frameworks derived from the folding studies of bacterial RNase P RNA.
authors.affiliation: Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637, USA.
authors.forename: Nathan J
authors.initials: NJ
authors.lastname: Baird
authors.forename: Xing-Wang
authors.initials: XW
authors.lastname: Fang
authors.forename: Narayanan
authors.initials: N
authors.lastname: Srividya
authors.forename: Tao
authors.initials: T
authors.lastname: Pan
authors.forename: Tobin R
authors.initials: TR
authors.lastname: Sosnick
mesh_terms: D003198:Computer Simulation; D004789:Enzyme Activation; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D043262:Ribonuclease P / Q000737:chemistry* / Q000648:ultrastructure*
chemical_list: D043262:Ribonuclease P