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Correlating Structural Dynamics and Function in Single Ribozyme Molecules

Zhuang, Xiaowei, Kim, Harold, Pereira, Miguel J. B., Babcock, Hazen P., Walter, Nils G., Chu, Steven·2002·Science

Abstract

We have studied the correlation between structural dynamics and function of the hairpin ribozyme. The enzyme-substrate complex exists in either docked (active) or undocked (inactive) conformations. Using single-molecule fluorescence methods, we found complex structural dynamics with four docked states of distinct stabilities and a strong memory effect where each molecule rarely switches between different docked states. We also found substrate cleavage to be rate-limited by a combination of conformational transitions and reversible chemistry equilibrium. The complex structural dynamics quantitatively explain the heterogeneous cleavage kinetics common to many catalytic RNAs. The intimate coupling of structural dynamics and function is likely a general phenomenon for RNA.

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Metadata

Authors
Zhuang, X., Kim, H., Pereira, M. J. B., Babcock, H. P., Walter, N. G., & Chu, S.
Venue
Science
Published
2002-05-24
Volume
296
Issue
5572
Pages
1473-1476
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2102032812
Cited by
512
References
0
FWCI
13.18
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Correlating Structural Dynamics and Function in Single Ribozyme Molecules. https://app.cochat.ai/papers/10.1126/science.1069013
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Zhuang, X., Kim, H., Pereira, M. J. B., Babcock, H. P., Walter, N. G., & Chu, S. (2002). Correlating Structural Dynamics and Function in Single Ribozyme Molecules. Science. https://doi.org/10.1126/science.1069013

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.