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

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 prot...

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Detalles Bibliográficos
Autores principales: Dubois, Cécile, Herrada, Isaline, Barthe, Philippe, Roumestand, Christian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7731413/
https://www.ncbi.nlm.nih.gov/pubmed/33256081
http://dx.doi.org/10.3390/molecules25235551

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7731413/
https://www.ncbi.nlm.nih.gov/pubmed/33256081
http://dx.doi.org/10.3390/molecules25235551

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