Caricamento...
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...
Salvato in:
| Pubblicato in: | Proc Natl Acad Sci U S A |
|---|---|
| Autori principali: | , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
2018
|
| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5939115/ https://ncbi.nlm.nih.gov/pubmed/29666248 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1803642115 |
| Tags: |
Aggiungi Tag
Nessun Tag, puoi essere il primo ad aggiungerne! !
|