Effects of mutations on the molecular dynamics of oxygen escape from the dimeric hemoglobin of Scapharca inaequivalvis [v1; ref status: indexed, http://f1000r.es/52d]
Like many hemoglobins, the structure of the dimeric hemoglobin from the clam Scapharca inaequivalvis is a “closed bottle” since there is no direct tunnel from the oxygen binding site on the heme to the solvent. The proximal histidine faces the dimer interface, which consists of the E and F helicies...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
F1000 Research Ltd
2015-03-01
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| Series: | F1000Research |
| Subjects: | |
| Online Access: | http://f1000research.com/articles/4-65/v1 |