BICH 410 Lecture Notes - Lecture 15: Hemoglobin, Conformational Change, Hydrophile
Document Summary
Cooperativity is designed to release o2 at low pressures. Inspired air has a high po2 binding while cytosol has a low po2 release. By promoting structural changes that enhance or diminish hb"s af nity for o2. The conformational change changes the af nity hemoglobin has for o2 -> this relates to the t-state and r-state. Strong points of contact between the beta and alpha dimers (where hydrophobic interactions and ionic interactions occur) These ionic & hydrogen bonds can be affected by ph but the hydrophobic interactions go on unaffected. The rst binding of oxygen is the hardest because of the amount of energy that. Rst molecule has to use to cause an overall structural change of the hemoglobin. The movement with one binding is about 15 degrees (just rotation) This is representative of a fairly massive change in the shape of hemoglobin. The only actual change is the dimer dimer hydrophilic interactions.
