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Protonation states of histidine and other key residues in deoxy normal human adult hemoglobin by neutron protein crystallography
The protonation states of the histidine residues key to the function of deoxy (T-state) human hemoglobin have been investigated using neutron protein crystallography. These residues can reversibly bind protons, thereby regulating the oxygen affinity of hemoglobin. By examining the OMIT F (o) − F (c)...
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| Hlavní autoři: | , , , , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
International Union of Crystallography
2010
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2967419/ https://ncbi.nlm.nih.gov/pubmed/21041929 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S0907444910025448 |
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