Kinetic intermediates in RNA folding. Export

@article{zarrinkar94, abstract = {The folding pathways of large, highly structured RNA molecules are largely unexplored. Insight into both the kinetics of folding and the presence of intermediates was provided in a study of the Mg(2+)-induced folding of the Tetrahymena ribozyme by hybridization of complementary oligodeoxynucleotide probes. This RNA folds via a complex mechanism involving both Mg(2+)-dependent and Mg(2+)-independent steps. A hierarchical model for the folding pathway is proposed in which formation of one helical domain (P4-P6) precedes that of a second helical domain (P3-P7). The overall rate-limiting step is formation of P3-P7, and takes place with an observed rate constant of 0.72 +/- 0.14 minute-1. The folding mechanism of large RNAs appears similar to that of many multidomain proteins in that formation of independently stable substructures precedes their association into the final conformation.}, address = {Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.}, author = {Zarrinkar, P. P. and Williamson, J. R.}, citeulike-article-id = {2857756}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/8052848}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=8052848}, day = {12}, issn = {0036-8075}, journal = {Science (New York, N.Y.)}, keywords = {folding, ribozyme, tetrayhmena}, month = {August}, number = {5174}, pages = {918--924}, posted-at = {2008-06-02 20:55:15}, priority = {5}, title = {Kinetic intermediates in RNA folding.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/8052848}, volume = {265}, year = {1994} }

TY - JOUR ID - zarrinkar94 L3 - citeulike-article-id:2857756 N2 - The folding pathways of large, highly structured RNA molecules are largely unexplored. Insight into both the kinetics of folding and the presence of intermediates was provided in a study of the Mg(2+)-induced folding of the Tetrahymena ribozyme by hybridization of complementary oligodeoxynucleotide probes. This RNA folds via a complex mechanism involving both Mg(2+)-dependent and Mg(2+)-independent steps. A hierarchical model for the folding pathway is proposed in which formation of one helical domain (P4-P6) precedes that of a second helical domain (P3-P7). The overall rate-limiting step is formation of P3-P7, and takes place with an observed rate constant of 0.72 +/- 0.14 minute-1. The folding mechanism of large RNAs appears similar to that of many multidomain proteins in that formation of independently stable substructures precedes their association into the final conformation. IS - 5174 JF - Science (New York, N.Y.) SN - 0036-8075 AD - Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139. EP - 924 TI - Kinetic intermediates in RNA folding. VL - 265 SP - 918 KW - folding KW - ribozyme KW - tetrayhmena AU - Zarrinkar, PP AU - Williamson, JR PY - 1994/08/12/ UR - http://view.ncbi.nlm.nih.gov/pubmed/8052848 ER -