title: Time-resolved NMR studies of RNA folding.
abstract: The application of real-time NMR experiments to the study of RNA folding, as reviewed in this article, is relatively new. For many RNA folding events, current investigations suggest that the time scales are in the second to minute regime. In addition, the initial investigations suggest that different folding rates are observed for one structural transition may be due to the hierarchical folding units of RNA. Many of the experiments developed in the field of NMR of protein folding cannot directly be transferred to RNA: hydrogen exchange experiments outside the spectrometer cannot be applied since the intrinsic exchange rates are too fast in RNA, relaxation dispersion experiments on the other require faster structural transitions than those observed in RNA. On the other hand, information derived from time-resolved NMR experiments, namely the acquisition of native chemical shifts, can be readily interpreted in light of formation of a single long-range hydrogen bonding interaction. Together with mutational data that can readily be obtained for RNA and new ligation technologies that enhance site resolution even further, time-resolved NMR may become a powerful tool to decipher RNA folding. Such understanding will be of importance to understand the functions of coding and non-coding RNAs in cells.
authors.affiliation: Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str 7, Frankfurt, Germany.
authors.forename: Boris
authors.initials: B
authors.lastname: Fürtig
authors.forename: Janina
authors.initials: J
authors.lastname: Buck
authors.forename: Vijayalaxmi
authors.initials: V
authors.lastname: Manoharan
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Bermel
authors.forename: Andres
authors.initials: A
authors.lastname: Jäschke
authors.forename: Philipp
authors.initials: P
authors.lastname: Wenter
authors.forename: Stefan
authors.initials: S
authors.lastname: Pitsch
authors.forename: Harald
authors.initials: H
authors.lastname: Schwalbe
mesh_terms: D055592:Biophysical Phenomena; D001703:Biophysics; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D012313:RNA / Q000737:chemistry* / Q000378:metabolism; D043262:Ribonuclease P / Q000737:chemistry / Q000378:metabolism; D013816:Thermodynamics
chemical_list: D008024:Ligands; D012313:RNA; D043262:Ribonuclease P