15N CEST data and traditional model-free analysis capture fast internal dynamics of DJ-1

Jonathan Catazaro, Tessa Andrews, Nicole M. Milkovic, Jiusheng Lin, Austin J. Lowe, Mark A. Wilson, Robert Powers

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Previous studies have shown that relaxation parameters and fast protein dynamics can be quickly elucidated from 15N-CEST experiments [1]. Longitudinal R1 and transverse R2 values were reliably derived from fitting of CEST profiles. Herein we show that 15N-CEST experiments and traditional modelfree analysis provide the internal dynamics of three states of human protein DJ-1 at physiological temperature. The chemical exchange profiles show the absence of a minor state conformation and, in conjunction with 1H-15N NOEs, show increased mobility. R1 and R2 values remained relatively unchanged at the three naturally occurring oxidation states of DJ-1, but exhibit striking NOE differences. The NOE data was, therefore, essential in determining the internal motions of the DJ-1 proteins. To the authors' knowledge, we present the first study that combines 15N CEST data with traditional model-free analyses in the study of a biological system and affirm that more ‘lean’ model-free approaches should be used cautiously.

Original languageEnglish (US)
Pages (from-to)24-28
Number of pages5
JournalAnalytical Biochemistry
StatePublished - Feb 1 2018


  • CEST
  • DJ-1
  • NMR
  • Protein dynamics

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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