Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway.
Apomyoglobin folding proceeds through a molten globule intermediate (low-salt form; I1) that has been characterized by equilibrium (pH 4) and kinetic (pH 6) folding experiments. Of the eight alpha-helices in myoglobin, three (A, G, and H) are structured in I1, while the rest appear to be unfolded. H...
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| Publicado no: | Proc Natl Acad Sci U S A |
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| Principais autores: | , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
1995
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC41711/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7777528/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.92.12.5446 |
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