Related ArticlesReal-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]
[NMR paper] Real-time protein NMR spectroscopy and investigation of assisted protein folding.
Real-time protein NMR spectroscopy and investigation of assisted protein folding.
Real-time protein NMR spectroscopy and investigation of assisted protein folding.
Biochim Biophys Acta. 2014 Dec 10;
Authors: Kumar A, Balbach J
Abstract
BACKGROUND: During protein folding reactions toward the native structure, short-lived intermediate states can be populated. Such intermediates expose hydrophobic patches and can self-associate leading to non-productive protein misfolding. A major focus of current research is the characterization...
nmrlearner
Journal club
0
12-17-2014 09:43 PM
Real-time protein NMR spectroscopy and investigation of assisted protein folding
Real-time protein NMR spectroscopy and investigation of assisted protein folding
Publication date: Available online 11 December 2014
Source:Biochimica et Biophysica Acta (BBA) - General Subjects</br>
Author(s): Amit Kumar , Jochen Balbach</br>
Background During protein folding reactions toward the native structure, short-lived intermediate states can be populated. Such intermediates expose hydrophobic patches and can self-associate leading to non-productive protein misfolding. A major focus of current research is the characterization of short-lived intermediates...
nmrlearner
Journal club
0
12-12-2014 11:30 AM
[NMR paper] Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy.
Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy.
Related Articles Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy.
Chembiochem. 2013 Jun 6;
Authors: Amata I, Maffei M, Igea A, Gay M, Vilaseca M, Nebreda AR, Pons M
Abstract
Intrinsically disordered regions (IDRs) are preferred sites for post-translational modifications essential for regulating protein function. The enhanced local...
nmrlearner
Journal club
0
06-08-2013 02:18 PM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
Abstract It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all detectable species. The analysis was carried out using experimental data obtained during aggregation of the 10.4 kDa Crh protein, which has been shown to involve a partially unfolded intermediate...
nmrlearner
Journal club
0
01-27-2011 04:31 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
J Biomol NMR. 2011 Jan 21;
Authors: Etzkorn M, Böckmann A, Baldus M
It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all...
nmrlearner
Journal club
0
01-22-2011 01:52 PM
[NMR paper] Protein folding studied by real-time NMR spectroscopy.
Protein folding studied by real-time NMR spectroscopy.
Related Articles Protein folding studied by real-time NMR spectroscopy.
Methods. 2004 Sep;34(1):65-74
Authors: Zeeb M, Balbach J
Real-time NMR spectroscopy developed to a generally applicable method to follow protein folding reactions. It combines the access to high resolution data with kinetic experiments allowing very detailed insights into the development of the protein structure during different steps of folding. The present review concentrates mainly on the progress of real-time NMR...
nmrlearner
Journal club
0
11-24-2010 10:01 PM
[NMR paper] Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
Related Articles Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
J Mol Biol. 2003 May 16;328(5):1161-71
Authors: Mizuguchi M, Kroon GJ, Wright PE, Dyson HJ
At low ionic strength, apoplastocyanin forms an unfolded state under non-denaturing conditions. The refolding of this state is sufficiently slow to allow real-time NMR experiments to be performed. Folding of apoplastocyanin, initiated by the addition of salt and followed by real-time 2D 1H-15N...
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[NMR paper] Following protein folding in real time using NMR spectroscopy.
Following protein folding in real time using NMR spectroscopy.
Related Articles Following protein folding in real time using NMR spectroscopy.
Nat Struct Biol. 1995 Oct;2(10):865-70
Authors: Balbach J, Forge V, van Nuland NA, Winder SL, Hore PJ, Dobson CM
The refolding of apo bovine alpha-lactalbumin has been monitored in real time by NMR spectroscopy following rapid in situ dilution of a chemically denatured state. By examining individual resonances in the time-resolved NMR spectra, the native state has been shown to emerge in a cooperative...
Real-Time Analysis of Folding upon Binding of a Disordered Protein by using Dissolution DNP NMR Spectroscopy.
Linear Mode
