Does native state topology determine the RNA folding mechanism?

Recent studies in protein folding suggest that native state topology plays a dominant role in determining the folding mechanism, yet an analogous statement has not been made for RNA, most likely due to the strong coupling between the ionic environment and conformational energetics that make RNA folding more complex than protein folding. Applying a distributed computing architecture to sample nearly 5000 complete tRNA folding events using a minimalist, atomistic model, we have characterized the role of native topology in tRNA folding dynamics: the simulated bulk folding behavior predicts well the experimentally observed folding mechanism. In contrast, single-molecule folding events display multiple discrete folding transitions and compose a largely diverse, heterogeneous dynamic ensemble. This both supports an emerging view of heterogeneous folding dynamics at the microscopic level and highlights the need for single-molecule experiments and both single-molecule and bulk simulations in interpreting bulk experimental measurements. (C) 2004 Elsevier Ltd. All rights reserved.
Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
Issue Date
2004-04
Language
English
Keywords

TRANSITION-STATE; COMPUTER-SIMULATION; GLOBULAR-PROTEINS; YEAST TRNA(PHE); SH3 DOMAINS; DYNAMICS; KINETICS; MAGNESIUM(II); FLUCTUATIONS; LANDSCAPES

Citation

JOURNAL OF MOLECULAR BIOLOGY, v.337, no.4, pp.789 - 797

ISSN
0022-2836
DOI
10.1016/j.jmb.2004.02.024
URI
http://hdl.handle.net/10203/225421
Appears in Collection
CH-Journal Papers(저널논문)
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