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Article dans une revue

Combining High-Pressure Perturbation with NMR Spectroscopy for a Structural and Dynamical Characterization of Protein Folding Pathways

Abstract : High-hydrostatic pressure is an alternative perturbation method that can be used to destabilize globular proteins. Generally perfectly reversible, pressure exerts local effects on regions or domains of a protein containing internal voids, contrary to heat or chemical denaturant that destabilize protein structures uniformly. When combined with NMR spectroscopy, high pressure (HP) allows one to monitor at a residue-level resolution the structural transitions occurring upon unfolding and to determine the kinetic properties of the process. The use of HP-NMR has long been hampered by technical difficulties. Owing to the recent development of commercially available high-pressure sample cells, HP-NMR experiments can now be routinely performed. This review summarizes recent advances of HP-NMR techniques for the characterization at a quasi-atomic resolution of the protein folding energy landscape.
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https://hal.umontpellier.fr/hal-03472278
Contributeur : Philippe BARTHE Connectez-vous pour contacter le contributeur
Soumis le : jeudi 9 décembre 2021 - 11:43:29
Dernière modification le : mardi 17 mai 2022 - 03:51:26

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Cécile Dubois, Isaline Herrada, Philippe Barthe, Christian Roumestand. Combining High-Pressure Perturbation with NMR Spectroscopy for a Structural and Dynamical Characterization of Protein Folding Pathways. Molecules, MDPI, 2020, 25 (23), pp.5551. ⟨10.3390/molecules25235551⟩. ⟨hal-03472278⟩

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