A2 Refereed review article in a scientific journal
Chemical models for ribozyme action
Authors: Lonnberg T, Lonnberg H
Publisher: CURRENT BIOLOGY LTD
Publication year: 2005
Journal:: Current Opinion in Chemical Biology
Journal name in source: CURRENT OPINION IN CHEMICAL BIOLOGY
Journal acronym: CURR OPIN CHEM BIOL
Volume: 9
Issue: 6
First page : 665
Last page: 673
Number of pages: 9
ISSN: 1367-5931
DOI: https://doi.org/10.1016/j.cbpa.2005.10.004
Abstract
Mechanistic studies of the action of catalytic ribonucleic acids, ribozymes, are highly challenging, because even a slight structural change can dramatically affect the chain folding. This, in turn, alters the binding properties of the catalytic core, making identification of the real origin of the observed influence on rate difficult. Unambiguous structure-reactivity correlations based on studies with structurally simplified chemical models may help to distinguish between alternative mechanistic interpretations. The results of such model studies are reviewed. The topics include intramolecular cleavage of RNA phosphodiester bonds by solvent-derived species, general acids/bases and metal ions, effect of molecular environment on their hydrolytic stability and trinucleoside monophosphates as models for large ribozymes.
Mechanistic studies of the action of catalytic ribonucleic acids, ribozymes, are highly challenging, because even a slight structural change can dramatically affect the chain folding. This, in turn, alters the binding properties of the catalytic core, making identification of the real origin of the observed influence on rate difficult. Unambiguous structure-reactivity correlations based on studies with structurally simplified chemical models may help to distinguish between alternative mechanistic interpretations. The results of such model studies are reviewed. The topics include intramolecular cleavage of RNA phosphodiester bonds by solvent-derived species, general acids/bases and metal ions, effect of molecular environment on their hydrolytic stability and trinucleoside monophosphates as models for large ribozymes.
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