[NMR paper] Refolding of cold denatured barstar induced by radio frequency heating - new method to study protein folding by real-time NMR spectroscopy.
Related ArticlesRefolding 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 lossy aqueous samples, refolding of barstar from its cold denatured state can be followed by real-time NMR spectroscopy. Since temperature-induced unfolding and refolding is reversible for this double mutant, multiple cycling can be utilized to obtain 2D real-time NMR data. Barstar contains two proline residues that adopt a mix of cis and trans conformations in the low temperature-unfolded state, which can potentially induce multiple folding pathways. The high time resolution real-time 2D-NMR measurements reported here show evidence for multiple folding pathways related to proline isomerization, and stable intermediates are populated. By application of advanced heating cycles and state-correlated spectroscopy, an alternative folding pathway circumventing the rate limiting cis-trans isomerization could be observed. The kinetic data revealed intermediates on both, the slow and the fast folding pathway.
PMID: 32744407 [PubMed - as supplied by publisher]
[NMR paper] Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Related Articles Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Angew Chem Int Ed Engl. 2001 Nov 19;40(22):4248-4251
Authors: Wirmer J, Kühn T, Schwalbe H
Abstract
Aspects of the structure of the intermediate populated after 200 ms in the Ca2+ -induced refolding of ?-lactalbumin have been...
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05-03-2018 06:46 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
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...
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08-22-2010 03:50 AM
[NMR paper] Real-time NMR studies on a transient folding intermediate of barstar.
Real-time NMR studies on a transient folding intermediate of barstar.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Real-time NMR studies on a transient folding intermediate of barstar.
Protein Sci. 1999 Jun;8(6):1286-91
Authors: Killick TR, Freund SM, Fersht AR
The refolding of barstar, the intracellular...
Refolding of cold denatured barstar induced by radio frequency heating - new method to study protein folding by real-time NMR spectroscopy.
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