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Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through and obligatory intermediate.
Folding of apomyoglobin is characterized by formation of a compact intermediate that contains substantial helicity. To determine whether this intermediate is obligatory or whether the protein can fold directly into the native state via an alternate parallel pathway, we have combined quench-flow hydr...
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| Main Authors: | , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
Cold Spring Harbor Laboratory Press
1999
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| Assuntos: | |
| Acceso en liña: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2144105/ https://ncbi.nlm.nih.gov/pubmed/10210182 |
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