Real-Time Analysis of Folding upon Binding of a Disordered Protein by using Dissolution DNP NMR Spectroscopy.
 

Real-Time Analysis of Folding upon Binding of a Disordered Protein by using Dissolution DNP NMR Spectroscopy.

Related Articles Real-Time Analysis of Folding upon Binding of a Disordered Protein by using Dissolution DNP NMR Spectroscopy.

Angew Chem Int Ed Engl. 2017 May 16;:

Authors: Ragavan M, Iconaru LI, Park CG, Kriwacki RW, Hilty C

Abstract
The kinase inhibitory domain of the cell cycle regulatory protein p27(Kip1) (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) C NMR 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.


PMID: 28508552 [PubMed - as supplied by publisher]



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