[NMR paper] Combining High-Pressure Perturbation with NMR Spectroscopy for a Structural and Dynamical Characterization of Protein Folding Pathways.
Combining High-Pressure Perturbation with NMR Spectroscopy for a Structural and Dynamical Characterization of Protein Folding Pathways.
Related Articles Combining High-Pressure Perturbation with NMR Spectroscopy for a Structural and Dynamical Characterization of Protein Folding Pathways.
Molecules. 2020 Nov 26;25(23):
Authors: Dubois C, Herrada I, Barthe P, Roumestand C
Abstract
High-hydrostatic pressure is an alternative perturbation method that can be used to destabilize globular proteins. Generally perfectly reversible,...
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[ASAP] Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR
Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR
Cyril Charlier, Joseph M. Courtney, T. Reid Alderson, Philip Anfinrud, Ad Bax
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.8b04833/20180625/images/medium/ja-2018-04833s_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.8b04833
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/Wf5C6etrn-c
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[NMR paper] Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR.
Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR.
J Am Chem Soc. 2018 Jun 20;:
Authors: Charlier C, Courtney JM, Alderson TR, Anfinrud P, Bax A
Abstract
Novel pressure-jump NMR hardware permits direct observation of protein NMR spectra during a cyclically repeated protein folding process. While protein...
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06-21-2018 10:11 PM
[NMR paper] Monitoring protein folding through high pressure NMR spectroscopy.
Monitoring protein folding through high pressure NMR spectroscopy.
Monitoring protein folding through high pressure NMR spectroscopy.
Prog Nucl Magn Reson Spectrosc. 2017 Nov;102-103:15-31
Authors: Roche J, Royer CA, Roumestand C
Abstract
High-pressure is a well-known perturbation method used to destabilize globular proteins. It is perfectly reversible, which is essential for a proper thermodynamic characterization of a protein equilibrium. In contrast to other perturbation methods such as heat or chemical denaturant that...
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11-22-2017 02:01 PM
[NMR paper] Monitoring Hydrogen Exchange During Protein Folding by Fast Pressure Jump NMR Spectroscopy.
Monitoring Hydrogen Exchange During Protein Folding by Fast Pressure Jump NMR Spectroscopy.
Related Articles Monitoring Hydrogen Exchange During Protein Folding by Fast Pressure Jump NMR Spectroscopy.
J Am Chem Soc. 2017 Aug 02;:
Authors: Alderson TR, Charlier C, Torchia DA, Anfinrud P, Bax A
Abstract
A method is introduced that permits direct observation of the rates at which backbone amide hydrogens become protected from solvent exchange after rapidly dropping the hydrostatic pressure inside the NMR sample cell from denaturing...
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Monitoring Protein Folding Through High Pressure NMR Spectroscopy
Monitoring Protein Folding Through High Pressure NMR Spectroscopy
Publication date: Available online 2 June 2017
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Julien Roche, Catherine A. Royer, Christian Roumestand</br>
High-pressure is a well-known perturbation method used to destabilize globular proteins. It is perfectly reversible, which is essential for a proper thermodynamic characterization of a protein equilibrium. In contrast to other perturbation methods such as heat or chemical denaturant that destabilize protein structures...
[NMR paper] The Energetics of a Three-State Protein Folding System Probed by High-Pressure Relaxation Dispersion NMR Spectroscopy.
The Energetics of a Three-State Protein Folding System Probed by High-Pressure Relaxation Dispersion NMR Spectroscopy.
Related Articles The Energetics of a Three-State Protein Folding System Probed by High-Pressure Relaxation Dispersion NMR Spectroscopy.
Angew Chem Int Ed Engl. 2015 Sep 14;54(38):11157-11161
Authors: Tugarinov V, Libich DS, Meyer V, Roche J, Clore GM
Abstract
The energetic and volumetric properties of a three-state protein folding system, comprising a metastable triple mutant of the Fyn SH3 domain, have been...
Monitoring protein folding through high pressure NMR spectroscopy - ScienceDirect.com
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