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Folding of a universal ribozyme: the ribonuclease P RNA

Published online by Cambridge University Press:  12 October 2007

Nathan J. Baird ,
Xing-Wang Fang ,
Narayanan Srividya ,
Tao Pan  and
Tobin R. Sosnick
Nathan J. Baird
Affiliation:
Department of Chemistry, University of Chicago, Chicago, IL 60637, USA Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637, USA
Xing-Wang Fang
Affiliation:
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA
Narayanan Srividya
Affiliation:
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA
Tao Pan*
Affiliation:
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA
Tobin R. Sosnick*
Affiliation:
Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637, USA Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA
*
*Correspondence may be addressed to either T. Sosnick or T. Pan at: 929 E. 57th St., Chicago, IL 60637, USA.
*Correspondence may be addressed to either T. Sosnick or T. Pan at: 929 E. 57th St., Chicago, IL 60637, USA.
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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.

Type
Review Article
Information
Quarterly Reviews of Biophysics , Volume 40 , Issue 2 , May 2007 , pp. 113 - 161
Copyright
Copyright © Cambridge University Press 2007

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