Journal
ANNUAL REVIEW OF BIOPHYSICS, VOL 39
Volume 39, Issue -, Pages 61-77Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.biophys.093008.131334
Keywords
ribozyme; energy landscape; collapse transition; SAXS; single-molecule FRET; hydroxyl radical footprinting
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM060819, R01GM046686] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM060819, R01 GM046686] Funding Source: Medline
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Large noncoding RNAs fold into their biologically functional structures via compact yet disordered intermediates, which couple the stable secondary structure of the RNA with the emerging tertiary fold. The specificity of the collapse transition, which coincides with the assembly of helical domains, depends on RNA sequence and counterions. It determines the specificity of the folding pathways and the magnitude of the free energy barriers to the ensuing search for the native conformation. By coupling helix assembly with nascent tertiary interactions, compact folding intermediates in RNA also play a crucial role in ligand binding and RNA-protein recognition.
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