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- Publisher
- Springer Journals
- Copyright
- Copyright © 2000 by Nature America Inc.
- Subject
- Life Sciences; Life Sciences, general; Biochemistry, general; Protein Structure; Membrane Biology; Biological Microscopy
- ISSN
- 1545-9993
- eISSN
- 1545-9985
- DOI
- 10.1038/79575
- Publisher site
- See Article on Publisher Site
Abstract
Two generalizations can be drawn from the recent rapid progress in understanding RNA–protein interactions. First, there is a great diversity of observed protein and RNA structural motifs. Second, formation of almost every RNA–protein complex that has been characterized involves conformational changes in the protein, the RNA, or both. The role of these conformational changes in the biological function of RNA–protein complexes is not at all clear. Whether or not conformational changes are a critical feature of ribonucleoprotein complex assembly or are an unimportant mechanistic detail, the ubiquity of these changes warrants careful consideration of their implications.
Journal
Nature Structural & Molecular Biology – Springer Journals
Published: Oct 1, 2000