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- W66884600 abstract "Upon dissociation of oxygen or carbon monoxide hemoglobin undergoes a series of conformational changes that are responsible for its cooperative behavior. X-ray structural studies show that these changes include a displacement of the iron from the heme plane and a tilt of the proximal histidine associated with a shift in the F helix (1–3). This shift destabilizes the intersubunit bonding between α β dimers, and after dissociation of one or two ligands the strain at the interface is sufficient to cause a transition from the R quaternary structure to the T quaternary structure." @default.
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- W66884600 date "1987-01-01" @default.
- W66884600 modified "2023-09-23" @default.
- W66884600 title "Dynamics of Structural Changes in Hemoglobin" @default.
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- W66884600 doi "https://doi.org/10.1007/978-3-642-71705-5_5" @default.
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