Multidimensional NMR intrinsically provides multiple probes that can be used for deciphering the folding pathways of proteins: NH amide and C?H? groups are strategically located on the backbone of the protein, while CH(3) groups, on the side-chain of methylated residues, are involved in important stabilizing interactions in the hydrophobic core. Combined with high hydrostatic pressure, these observables provide a powerful tool to explore the conformational landscapes of proteins. In the present...
[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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12-04-2020 03:46 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
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...
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06-02-2017 08:33 PM
[NMR paper] High-pressure NMR techniques for the study of protein dynamics, folding and aggregation.
High-pressure NMR techniques for the study of protein dynamics, folding and aggregation.
Related Articles High-pressure NMR techniques for the study of protein dynamics, folding and aggregation.
J Magn Reson. 2017 Apr;277:179-185
Authors: Nguyen LM, Roche J
Abstract
High-pressure is a well-known perturbation method used to destabilize globular proteins and dissociate protein complexes or aggregates. The heterogeneity of the response to pressure offers a unique opportunity to dissect the thermodynamic contributions to protein...
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04-02-2017 11:43 AM
High-pressure NMR techniques for the study of protein dynamics, folding and aggregation
High-pressure NMR techniques for the study of protein dynamics, folding and aggregation
Publication date: April 2017
Source:Journal of Magnetic Resonance, Volume 277</br>
Author(s): Luan M. Nguyen, Julien Roche</br>
High-pressure is a well-known perturbation method used to destabilize globular proteins and dissociate protein complexes or aggregates. The heterogeneity of the response to pressure offers a unique opportunity to dissect the thermodynamic contributions to protein stability. In addition, pressure perturbation is generally reversible, which is essential...
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03-30-2017 06:42 PM
Using High Pressure NMR to Study Folding Cooperativity and Kinetics of Protein L9
Using High Pressure NMR to Study Folding Cooperativity and Kinetics of Protein L9
Publication date: 3 February 2017
Source:Biophysical Journal, Volume 112, Issue 3, Supplement 1</br>
Author(s): Yi Zhang, Soichiro Kitazawa, Ivan Peran, Natalie Stenzoski, Scott McCallum, Daniel Raleigh, Catherine Royer</br>
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[NMR paper] Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.
Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.
Related Articles Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.
Subcell Biochem. 2015;72:261-278
Authors: Roche J, Dellarole M, Royer CA, Roumestand C
Abstract
Defining the physical-chemical determinants of protein folding and stability, under normal and pathological conditions has constituted a major subfield in biophysical chemistry for over 50 years. Although a great deal of...
Comparative Assessment of NMR Probes for the Experimental Description of Protein Folding Pathways with High-Pressure NMR
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