This simulator plots the hemoglobin-oxygen dissociation curve in real time, letting you see how saturation responds to changing oxygen partial pressure and how the curve shifts left or right under different pH and carbon dioxide conditions.
Adjust the oxygen partial pressure slider to trace saturation along the curve, then toggle pH or carbon dioxide levels to watch the Bohr effect shift the entire curve and reveal the corresponding change in P50.
Sliders control oxygen partial pressure, pH, and carbon dioxide level, with the resulting saturation percentage and P50 value updating live on the curve.
Myoglobin, the oxygen-storage protein in muscle, has only one binding site and no cooperative binding, so its dissociation curve is a simple hyperbola rather than an S-shape, a useful contrast for seeing what cooperativity actually adds.
This simulator plots the hemoglobin-oxygen dissociation curve in real time, letting you see how saturation responds to changing oxygen partial pressure and how the curve shifts left or right under different pH and carbon dioxide conditions.
This simulator plots the hemoglobin-oxygen dissociation curve in real time, letting you see how saturation responds to changing oxygen partial pressure and how the curve shifts left or right under different pH and carbon dioxide conditions.
Adjust the oxygen partial pressure slider to trace saturation along the curve, then toggle pH or carbon dioxide levels to watch the Bohr effect shift the entire curve and reveal the corresponding change in P50.
Myoglobin, the oxygen-storage protein in muscle, has only one binding site and no cooperative binding, so its dissociation curve is a simple hyperbola rather than an S-shape, a useful contrast for seeing what cooperativity actually adds.