Entropic stabilization of the folded states of RNA due to macromolecular crowding
Biophysical Reviews, ISSN: 1867-2469, Vol: 5, Issue: 2, Page: 225-232
2013
- 21Citations
- 18Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations21
- Citation Indexes21
- 21
- CrossRef15
- Captures18
- Readers18
- 18
Review Description
We review the effects of macromolecular crowding on the folding of RNA by considering the simplest scenario when excluded volume interactions between crowding particles and RNA dominate. Using human telomerase enzyme as an example, we discuss how crowding can alter the equilibrium between pseudoknot and hairpin states of the same RNA molecule-a key aspect of crowder-RNA interactions. We summarize data showing that the crowding effect is significant only if the size of the spherical crowding particle is smaller than the radius of gyration of the RNA in the absence of crowding particles. The implication for function of the wild type and mutants of human telomerase is outlined by using a relationship between enzyme activity and its conformational equilibrium. In addition, we discuss the interplay between macromolecular crowding and ionic strength of the RNA buffer. Finally, we briefly review recent experiments which illustrate the connection between excluded volume due to macromolecular crowding and the thermodynamics of RNA folding. © 2013 International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag Berlin Heidelberg.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84877022922&origin=inward; http://dx.doi.org/10.1007/s12551-013-0119-x; http://www.ncbi.nlm.nih.gov/pubmed/28510164; http://link.springer.com/10.1007/s12551-013-0119-x; https://dx.doi.org/10.1007/s12551-013-0119-x; https://link.springer.com/article/10.1007/s12551-013-0119-x
Springer Science and Business Media LLC
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