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Structural characterization of partially folded intermediates of apomyoglobin H64F
We present a detailed investigation of unfolded and partially folded states of a mutant apomyoglobin (apoMb) where the distal histidine has been replaced by phenylalanine (H64F). Previous studies have shown that substitution of His64, located in the E helix of the native protein, stabilizes the equi...
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| Autors principals: | , , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Cold Spring Harbor Laboratory Press
2008
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2222724/ https://ncbi.nlm.nih.gov/pubmed/18227434 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.073187208 |
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