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Ruggedness in the folding landscape of protein L
By exploring the folding pathways of the B1 domain of protein L with a series of equilibrium and rapid kinetic experiments, we have found its unfolded state to be more complex than suggested by two-state folding models. Using an ultrarapid mixer to initiate protein folding within ∼2–4 microseconds,...
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| Główni autorzy: | , , , , , , , , , , , |
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| Format: | Artigo |
| Język: | Inglês |
| Wydane: |
HFSP Publishing
2008
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| Hasła przedmiotowe: | |
| Dostęp online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2645578/ https://ncbi.nlm.nih.gov/pubmed/19436489 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.2976/1.3013702 |
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