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Dynamics of equilibrium structural fluctuations of apomyoglobin measured by fluorescence correlation spectroscopy
The spectra of equilibrium chain conformation fluctuations of apomyoglobin (apoMb) as a function of folding, from the acid-denatured state at pH 2.6 through the stable molten globule state pH ≈ 4.1 to the folded state at pH 6.3, are reported, as measured by fluorescence correlation spectroscopy. The...
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| Autores principales: | , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
National Academy of Sciences
2007
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1965535/ https://ncbi.nlm.nih.gov/pubmed/17556539 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0704073104 |
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