Question

Draw the hyperbolic curve of Mb-O2 binding, the hyperbolic curve of Hb-O2 binding without 2,3 BPG and the sigmoidal curve of Hb-O2 binding with 2,3 BPG. Understand how the curve explains the affinity difference and Hb cooperative binding.

Answer 1

@ Hb - Og bonding curve -- [without as Bral ② Mb-O2 binding curve e Oxyhex moglobin Fractional saturation of Myoglobin Foclonal salaatin NYIA 1 0 10 TO 20 90 100 20 30 40 50 60 po (Tm 19) 1026 to 50 €CYO 2090 PO, (mmHg) 3 Mb- O, binding curve saluration of Oxyhai moglobin Fractional 0 ge 10 10 20 30 40 50 e 70 70 po, (mmHg) -

2,3 B bep only binds with hemoglobin not with myoglobin berause it has only one subunit ciso also called monomer wheros hemoglobin has 4 subunit or monomer. The main difference of mboo dissociation curre is hyperbolic bul 16 - O₂ dissociation curve is a sigmoidal curve o ut for to not exist - De dry haemoglobin will long time because of unstable nature of t state So hemoglobin has a tendency to bind with O₂ 2- 3 Bar bind with ham hemoglobin and stable it in T state. C Only 8 % of Oq relesed by the pure hea hemoglobin to the tissue whereas 66%. O, releged for the fissue by 2,3 BAG 1. That is why hemoglobin is more used in between tissues and in Alto our respiratory organ ie lungs than myoglobin - Hb cooperative binding Cooperative binding sefers to the interaction between molecules which is in a stable physical association between those molecules. 1 402 molecule can bind up with each hati hemoglobin. cooperativity between De binding site and hemoglobin deliver more O₂ to tissue.