The pK(a) of His-24 in the folding transition state of apomyoglobin
In native apomyoglobin, His-24 cannot be protonated, although at pH 4 the native protein forms a molten globule folding intermediate in which the histidine residues are readily protonated. The inability to protonate His-24 in the native protein dramatically affects the unfolding/refolding kinetics,...
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| Published in: | Proc Natl Acad Sci U S A |
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| Main Authors: | , , |
| Format: | Artigo |
| Language: | Inglês |
| Published: |
National Academy of Sciences
2001
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC33433/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11353859/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.111157998 |
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