Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell

In general, small proteins rapidly fold on the timescale of milliseconds or less. For proteins with a substantial volume difference between the folded and unfolded states, their thermodynamic equilibrium can be altered by varying the hydrostatic pressure. Using a pressure-sensitized mutant of ubiqui...

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Detalles Bibliográficos
Autores principales: Charlier, Cyril, Alderson, T. Reid, Courtney, Joseph M., Ying, Jinfa, Anfinrud, Philip, Bax, Adriaan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: National Academy of Sciences 2018
Materias:
PNAS Plus
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5939115/
https://www.ncbi.nlm.nih.gov/pubmed/29666248
http://dx.doi.org/10.1073/pnas.1803642115

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5939115/
https://www.ncbi.nlm.nih.gov/pubmed/29666248
http://dx.doi.org/10.1073/pnas.1803642115

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