The solution structural ensembles of RNA kink-turn motifs and their protein complexes

Xuesong Shi (Lead / Corresponding author), Lin Huang, David M. J. Lilley, Pehr B. Harbury (Lead / Corresponding author), Daniel Herschlag (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)
148 Downloads (Pure)


With the growing number of crystal structures of RNA and RNA-protein complexes, a critical next step is understanding the dynamic solution behavior of these entities in terms of conformational ensembles and energy landscapes. To this end, we have used X-ray scattering interferometry (XSI) to probe the ubiquitous RNA kink-turn motif and its complexes with the canonical kink-turn binding protein L7Ae. XSI revealed that the folded kink-turn is best described as a restricted conformational ensemble. The ions present in solution alter the nature of this ensemble, and protein binding can perturb the kink-turn ensemble without collapsing it to a unique state. This study demonstrates how XSI can reveal structural and ensemble properties of RNAs and RNA-protein complexes and uncovers the behavior of an important RNA-protein motif. This type of information will be necessary to understand, predict and engineer the behavior and function of RNAs and their protein complexes.

Original languageEnglish
Pages (from-to)146-152
Number of pages7
JournalNature Chemical Biology
Issue number3
Early online date4 Jan 2016
Publication statusPublished - Mar 2016


  • Base sequence
  • Interferometry
  • Molecular dynamics simulation
  • Molecular sequence data
  • Nucleic acid conformation
  • Nucleotide motifs
  • RNA
  • Scattering, Radiation
  • X-Rays
  • Journal article
  • Research support, N.I.H., Extramural
  • Research support, Non-U.S. Gov't


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