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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...
| Autores principales: | , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
National Academy of Sciences
2018
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| Materias: | |
| 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 |