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10.1016/j.bbagrm.2014.04.005 http://scihub22266oqcxt.onion/10.1016/j.bbagrm.2014.04.005 C4177941!4177941 !24727093     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24727093 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\24727093 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biochim+Biophys+Acta 2014 ; 1839 (10 ): 1030-1045 Nephropedia Template TP {{tp|p=24727093 |t=2014. Single-molecule studies of riboswitch folding |pdf=|usr=}}{{24727093 }} gab.com Text Single-molecule studies of riboswitch folding JO: Biochim Biophys Acta http://www.kidney.de/pget.php?&tw=1&pmid=24727093 #FOAvip The folding dynamics of riboswitches are central to their ability to modulate gene expression in response to environmental cues. In most cases, a structural competition between the formation of a ligand-binding aptamer and an expression platform (or some other competing off-state) determines the regulatory outcome. Here, we review single-molecule studies of riboswitch folding and function, predominantly carried out using single-molecule FRET or optical trapping approaches. Recent results have supplied new insights into riboswitch folding energy landscapes, the mechanisms of ligand binding, the roles played by divalent ions, the applicability of hierarchical folding models, and kinetic vs. thermodynamic control schemes. We anticipate that future work, based on improved data sets and potentially combining multiple experimental techniques, will enable the development of more complete models for complex RNA folding processes. This article is part of a Special Issue entitled: Riboswitches. Twit Text FOAVip Single-molecule studies of riboswitch folding ????Biochim Biophys Acta http://www.kidney.de/pget.php?&tw=1&pmid=24727093 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24727093 #FOAvip English Wikipedia <ref>{{Cite pmid|24727093 }}</ref> Single-molecule studies of riboswitch folding #MMPMID24727093 Savinov A ; Perez CF ; Block SM Biochim Biophys Acta 2014[Oct]; 1839 (10 ): 1030-1045 PMID24727093 show ga The folding dynamics of riboswitches are central to their ability to modulate gene expression in response to environmental cues. In most cases, a structural competition between the formation of a ligand-binding aptamer and an expression platform (or some other competing off-state) determines the regulatory outcome. Here, we review single-molecule studies of riboswitch folding and function, predominantly carried out using single-molecule FRET or optical trapping approaches. Recent results have supplied new insights into riboswitch folding energy landscapes, the mechanisms of ligand binding, the roles played by divalent ions, the applicability of hierarchical folding models, and kinetic vs. thermodynamic control schemes. We anticipate that future work, based on improved data sets and potentially combining multiple experimental techniques, will enable the development of more complete models for complex RNA folding processes. This article is part of a Special Issue entitled: Riboswitches. äSingle-molecule studies of riboswitch folding (epmc).pdf DeepDyve Pubget Overpricing