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Replacement of the Distal Histidine Reveals a Non-Canonical Heme Binding Site in a 2-on-2 Hemoglobin
Heme ligation in hemoglobin is typically assumed by the “proximal” histidine. Hydrophobic contacts, ionic interactions, and the ligation bond secure the heme between two α- helices denoted E and F. Across the hemoglobin superfamily, several proteins also use a “distal” histidine, making the native s...
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| Vydáno v: | Biochemistry |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2018
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6217817/ https://ncbi.nlm.nih.gov/pubmed/30213188 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.biochem.8b00752 |
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