This protein's diminished function in acidic conditions is known as the Bohr effect.
This protein's structure can be made more rigid with 2,3-diphosphoglycerate. Fetal versions of this protein contain a serine-143 instead of a histidine-143 that increases this protein's efficiency. Breaking the valine-tyrosine bond in this protein's Helix E and Helix F regions causes a conformation change. This protein's diminished function in acidic conditions is known as the Bohr effect. This protein is made up of four subunits, at the center of which is a porphyrin ring with an iron cation. A problem with this protein is its greater affinity for carbon monoxide than for oxygen. For 10 points, name this protein found in red blood cells.
This protein's structure can be made more rigid with 2,3-diphosphoglycerate.
hemoglobin