Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate
On exposure to mildly acidic conditions, apomyoglobin forms a partially folded intermediate, I. The A, B, G, and H helices are significantly structured in this equilibrium intermediate, whereas the remainder of the protein is largely unfolded. We report here the effects of mutations at helix pairing...
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| Опубликовано в:: | Proc Natl Acad Sci U S A |
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| Главные авторы: | , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
National Academy of Sciences
1999
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC26727/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10051585/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.96.5.2007 |
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