BIOCH200 Lecture Notes - Hemoglobin, Cooperative Binding, Myoglobin

• School: University of Alberta
• Department: Biochemistry
• Course: BIOCH200
• Professor: Walter Dixon

Document Summary

Bioch 200 protein struture and function (con"t) | (february 24, 2014: hyperbolic curve as to myoglobin like sigmoidal curve as to hemoglobin, hyperbolic curve of myoglobin is representative of constant affinity. Ligand affinity (kd) does not change: sigmoidal curve of hemoglobin is indicative of cooperative binding affinity. *deoxyhemoglobin has a lower affinity for oxygen than an oxyhemoglobin that still has a subunit available for oxygen binding. *the binding of each subsequent oxygen molecule to the hemoglobin protein increases the affinity of hemoglobin for oxygen. *remember that: myoglobin is important between tissues (mainly muscle tissue, hemoglobin is important for oxygen transport from the lungs to tissues, the two distinct structures of hemoglobin (hb, tense (t-state) *his residue in subunit is wedged between thr and pro in the subunit. Characteristic structure of deoxyhemoglobin: relaxed (r-state) *his residue in subunit is wedged in between 2 thr amino acids in the subunit.