Real-Time Analysis of Folding upon Binding of a Disordered Protein by Using Dissolution DNPNMR Spectroscopy. Academic Article uri icon


  • The kinase inhibitory domain of the cell cycle regulatory protein p27Kip1 (p27) was nuclear spin hyperpolarized using dissolution dynamic nuclear polarization (D-DNP). While intrinsically disordered in isolation, p27 adopts secondary structural motifs, including an -helical structure, upon binding to cyclin-dependent kinase 2 (Cdk2)/cyclin A. The sensitivity gains obtained with hyperpolarization enable the real-time observation of 13 CNMR signals during p27 folding upon binding to Cdk2/cyclin A on a time scale of several seconds. Time-dependent intensity changes are dependent on the extent of folding and binding, as manifested in differential spin relaxation. The analysis of signal decay rates suggests the existence of a partially folded p27 intermediate during the timescale of the D-DNP NMR experiment.

published proceedings

  • Angew Chem Int Ed Engl

altmetric score

  • 1.25

author list (cited authors)

  • Ragavan, M., Iconaru, L. I., Park, C., Kriwacki, R. W., & Hilty, C.

citation count

  • 27

publication date

  • January 2017