A2 Vertaisarvioitu katsausartikkeli tieteellisessä lehdessä
Chemical models for ribozyme action
Tekijät: Lonnberg T, Lonnberg H
Kustantaja: CURRENT BIOLOGY LTD
Julkaisuvuosi: 2005
Lehti:: Current Opinion in Chemical Biology
Tietokannassa oleva lehden nimi: CURRENT OPINION IN CHEMICAL BIOLOGY
Lehden akronyymi: CURR OPIN CHEM BIOL
Vuosikerta: 9
Numero: 6
Aloitussivu: 665
Lopetussivu: 673
Sivujen määrä: 9
ISSN: 1367-5931
DOI: https://doi.org/10.1016/j.cbpa.2005.10.004
Tiivistelmä
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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