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RNA structures and dynamics with Å resolution revealed by x-ray free-electron lasers
Open accessPublished version of a preprint
Abstract
RNA macromolecules, like proteins, fold to assume shapes that are intimately connected to their broadly recognized biological functions; however, because of their high charge and dynamic nature, RNA structures are far more challenging to determine. We introduce an approach that exploits the high brilliance of x-ray free-electron laser sources to reveal the formation and ready identification of angstrom-scale features in structured and unstructured RNAs. Previously unrecognized structural signatures of RNA secondary and tertiary structures are identified through wide-angle solution scattering experiments. With millisecond time resolution, we observe an RNA fold from a dynamically varying single strand through a base-paired intermediate to assume a triple-helix conformation. While the backbone orchestrates the folding, the final structure is locked in by base stacking. This method may help to rapidly characterize and identify structural elements in nucleic acids in both equilibrium and time-resolved experiments.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Advances in protein structure prediction and design
Kuhlman, B., & Bradley, P. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0163-x · Cited by 806
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Metadata
- Authors
- Zielinski, K. A., Sui, S., Pabit, S. A., Rivera, D. A., Wang, T., Hu, Q., Kashipathy, M. M., Lisova, S., Schaffer, C. B., Mariani, V., Hunter, M. S., Kupitz, C., Moss, F. R., Poitevin, F. P., Grant, T. D., & Pollack, L.
- Affiliations
- Cornell University (US)
- SLAC National Accelerator Laboratory (US)
- University at Buffalo, State University of New York (US)
- Corresponding author
- Pollack, Lois
- ORCID
- Venue
- Science Advances
- Published
- 2023-09-29
- Volume
- 9
- Issue
- 39
- Pages
- eadj3509-eadj3509
- ISSN
- 2375-2548 (ISSN-L)
- PMC
- PMC10530093
- OpenAlex
- W4387092066
- Cited by
- 17
- References
- 2
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 6
- FWCI
- 1.51
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Science Advances (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- Funders
- National Science Foundation (1930046, 1231306)
- U.S. Department of Energy (76SF00515, DE–AC02–76SF00515, AC02‐76SF00515, No. DE-AC02–76SF00515, Contract No. DE-AC02-76SF00515, DE-AC02-)
- Pfizer
- National Institutes of Health (1s10od012331-01, 1s10od025079-01, 1s10od028617-01, DE-AC02-76SF00515)
- Office of Science (AC02-76SF00515, DE-AC02-76SF0051 5, DE-AC02, 76SF00515)
- Natural Sciences and Engineering Research Council of Canada
- National Institute of General Medical Sciences (R01GM133998, P30GM133893, P41GM139687, R35GM122514)
- Basic Energy Sciences (DE-AC02, 76SF00515, Contract No. DE-AC02-76SF00515, AC02-76SF00515, DE-AC-02-76SF00515)
- SLAC National Accelerator Laboratory (DEAC02−76SF00515, AC02‐76SF00515, Contract No. DE-AC02-76SF00515)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- RNA structure, RNA dynamics, X-ray free-electron laser, RNA folding, triple helix, base pairing, base stacking, nucleic acid structure, time-resolved scattering
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