[NMR paper] Refolding of cold denatured barstar induced by radio frequency heating - new method to study protein folding by real-time NMR spectroscopy.
Refolding of cold denatured barstar induced by radio frequency heating - new method to study protein folding by real-time NMR spectroscopy.
Related Articles Refolding of cold denatured barstar induced by radio frequency heating - new method to study protein folding by real-time NMR spectroscopy.
Angew Chem Int Ed Engl. 2020 Aug 03;:
Authors: Pintér G, Schwalbe H
Abstract
The C40A/C82A double mutant of barstar has been shown to undergo cold denaturation above the water freezing point. By rapidly applying radio frequency power to...
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08-04-2020 12:56 PM
Real-Time Analysis of Folding upon Binding of a Disordered Protein by Using Dissolution DNP NMR Spectroscopy #DNPNMR
From The DNP-NMR Blog:
Real-Time Analysis of Folding upon Binding of a Disordered Protein by Using Dissolution DNP NMR Spectroscopy #DNPNMR
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Ragavan, M., et al., Real-Time Analysis of Folding upon Binding of a Disordered Protein by Using Dissolution DNP NMR Spectroscopy. Angew Chem Int Ed Engl, 2017. 56(25): p. 7070-7073.
https://www.ncbi.nlm.nih.gov/pubmed/28508552
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12-12-2017 02:12 AM
[NMR paper] 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...
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05-17-2017 12:46 PM
[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...
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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...
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12-12-2014 11:30 AM
[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...
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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...
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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...
New method to study protein folding by real-time NMR spectroscopy - Wiley
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