Question

3. Hemoglobin (Hb) is similar to Mb in that it binds O2. However, there are some distinct differences. Complete the table below to illustrate some of these differences. Hb Mb Function in mammals Highest level of structure (1º, 2º, etc.) Shape of binding curve (vs Poz) (sketch the curve in the box, label the axes, and write the name of the type of curve it is) Type of Curve: Type of Curve: Where it is found in mammals 4. Let's say that you have a solution of Hb, but the conditions are such that the monomers are separated from one another, but still retain their individual tertiary structures. a. Could the monomers still bind oxygen? Yes No No b. If so, how would the binding curve of the separated Hb monomers look? Sketch it below. Label the axes appropriately.

Answer 1

Mb Hb Function : Oxygen transport, found in red blood intéracellular sloroge site for oxygen in muscle cell Highest level of structure الي 4 cure %02 Saturation % O2 satural - - - 40 to 30 Partial pressure 80 Partial pressure (Tess) rectangular shope: hyperbodo shape: Sigmoid Jound in erythrocyte mammal" (Red blood cell) Muscle 4.) (a) yes monomer still bind with Oxygen, because tertiary Stoocture of haemoglobior are remarkably similar to that of myoglobin. and each subunit iß capable of binding a single molecule of oxygen - sigmoid curve cooperativity) Hyperbolic curve (no cooperativety) LOD + (b) 100 E-