Aarhus University Seal

15N-Detected TROSY NMR experiments to study large disordered proteins in high-field magnets

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review


  • Abhinav Dubey, Dana-Farber Cancer Institute, Harvard University
  • ,
  • Thibault Viennet
  • Sandeep Chhabra, Dana-Farber Cancer Institute, Harvard University
  • ,
  • Koh Takeuchi, University of Tokyo
  • ,
  • Hee Chan Seo, Dana-Farber Cancer Institute, University of Bergen
  • ,
  • Wolfgang Bermel, Bruker BioSpin GmbH, Germany
  • ,
  • Dominique P. Frueh, Johns Hopkins University
  • ,
  • Haribabu Arthanari, Dana-Farber Cancer Institute, Harvard University

Intrinsically disordered regions (IDRs) of proteins are critical in the regulation of biological processes but difficult to study structurally. Nuclear magnetic resonance (NMR) is uniquely equipped to provide structural information on IDRs at atomic resolution; however, existing NMR methods often pose a challenge for large molecular weight IDRs. Resonance assignment of IDRs using 15ND-detection was previously demonstrated and shown to overcome some of these limitations. Here, we improve the methodology by overcoming the need for deuterated buffers and provide better sensitivity and resolution at higher magnetic fields and physiological salt concentrations using transverse relaxation optimized spectroscopy (TROSY). Finally, large disordered regions with low sequence complexity can be assigned efficiently using these new methods as demonstrated by achieving near complete assignment of the 398-residue N-terminal IDR of the transcription factor NFAT1 harboring 18% prolines.

Original languageEnglish
JournalChemical Communications
Pages (from-to)9512-9515
Number of pages4
Publication statusPublished - 28 Jul 2022
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2022 The Royal Society of Chemistry.

See relations at Aarhus University Citationformats

ID: 339462695