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We found that the RNA is significantly more flexible in the absence of the 15.5K protein. Conformational transitions such as the interconversion between alternative purine stacking schemes, the loss of G-A base pairs, and the opening of the K-turn occur only in the free RNA. Furthermore, the stability of one canonical G-C base pair is influenced both by the binding of the 15.5K protein and the nature of the adjacent structural element in the RNA. We performed chemical RNA modification experiments and observed that the free RNA lacks secondary structure elements, a result in excellent agreement with the simulations. Based on these observations, we propose a protein-assisted RNA folding mechanism in which the RNA intrinsic flexibility functions as a catalyst.<\/jats:p>","DOI":"10.1261\/rna.7149605","type":"journal-article","created":{"date-parts":[[2005,1,19]],"date-time":"2005-01-19T03:22:57Z","timestamp":1106104977000},"page":"197-209","source":"Crossref","is-referenced-by-count":38,"title":["The snRNP 15.5K protein folds its cognate K-turn RNA: A combined theoretical and biochemical study"],"prefix":"10.1261","volume":"11","author":[{"given":"VLAD","family":"COJOCARU","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"STEPHANIE","family":"NOTTROTT","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"REINHARD","family":"KLEMENT","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"THOMAS M.","family":"JOVIN","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"246","published-online":{"date-parts":[[2005,1,18]]},"reference":[{"key":"2021112105393027000_11.2.197.1","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/S0166-1280(96)04995-0","volume":"423","year":"1998","journal-title":"J. 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