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Guanidine-unfolded state of ribonuclease A contains both fast- and slow-refolding species.
The kinetics of the refolding reaction of ribonuclease A from high concentrations of guanidine hydrochloride or urea are biphasic, and show two refolding reactions whose rates differ 450-fold at pH 5.8 and 25 degrees. Measurements of cytidine 2'-phosphate binding during refolding, after stopped...
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| Pubblicato in: | Proc Natl Acad Sci U S A |
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| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
1976
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC430405/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1064858/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.73.6.1853 |
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