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Probing the protein-folding mechanism using denaturant and temperature effects on rate constants
Protein folding has been extensively studied, but many questions remain regarding the mechanism. Characterizing early unstable intermediates and the high–free-energy transition state (TS) will help answer some of these. Here, we use effects of denaturants (urea, guanidinium chloride) and temperature...
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| Autores principales: | , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
National Academy of Sciences
2013
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3801023/ https://ncbi.nlm.nih.gov/pubmed/24043778 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1311948110 |
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