Myoglobin is a protein with a single haeme group, which binds oxygen inside our cells and makes it available for metabolism. Oxygen binding to myoglobin is described by a hyperbola. Haemoglobin consists of two ',"-protomers, each of the four proteins contains a haeme group. Binding of oxygen to one of these haeme groups increases the affinity of the remaining sites for oxygen; this cooperation results in an S-shaped (sigmoidal) binding curve. The shape of this curve is influenced by pH and the presence of 2,3-Bisphosphoglycerate (2,3-BPG). Mutations in the genes for either the '-or the "-subunits of haemoglobin can cause serious disease.
CITATION STYLE
Buxbaum, E. (2015). Hæmoglobin and Myoglobin: Cooperativity. In Fundamentals of Protein Structure and Function (pp. 163–184). Springer International Publishing. https://doi.org/10.1007/978-3-319-19920-7_7
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