Question

biochemistry concept I need help with. not a hw question.

HEMOGLOBIN Draw the oxygen-binding curve on the graph for A-normal hemoglobin, B normal hemoglobin when BPG levels double and c-a disease that causes high blood oxygenation but poor muscle oxygenation The disease is blocking | disease GPS from binding tightly hot Saluston sont Without BPG - an allotter inhibitor - hemoglobin will bind Oz and not Clease it in tissues. /B 2x BPG Binding curve shifts left POz (torr) Poor Oxygen in the blood. How does this mutation cause this? Draw Curve for Anormal hemogbbia, B-half BP6, and C-diowe. foox LBPS Bonal e disewa The mutation could be taking too much Ht from CO2/ Hoa lowering blood pH At low pH, hemoglobin Aside chains can be partially pratinated + reduce affinity ' for oxygen PO2 (tor) In a mutation where BPG activity increases, how does that work? Too much BPG a made, acting as an allosteric inhibitor, preventing Od 6:nding. So Or Cute Shifts cient

on our test our professor is going to ask us something along the lines of these questions but I just don't understand them even after reading the questions. I don't understand how to know when to shift the line to the right vs left.

Answer 1

To understand these questions you have to understand basic concept of shifting of HbA curve to right of left . Once you understand this concept you will be able to these questions easily. Firstly I have explained the basis and later Hb A problems. Hope this will help.

once you understand the concept . Then the factors cause shifting of curve to right of left .

a a firstly we have to understand anupt behind partial preome of og and y. saturation of 12b as Hb is a alusterie protein , it show sigmoidal caure - Cure for - cu or Noored ML. I HA j toot left to Presowe - lens require ht, sph, az BPL saturation - 8 nb O Paw .. lets assure this stored hs get sot saturated at training if this curre shift left if this curre sheft .. Right siche - at some partial arrine it now satureded 75% sunet partial pressure smary ¿ USA is only about 234. saturales, here a - tess setan of G- has been unloaded on shfa depend on ing required an MA cure to right ar left requirement of g Right Shift, 18% less requirie - Lett

Right shift- metabolically active cell has increased H+, decrease pH due to large amount of Co2 production, increase amount of 2,3 BPG.

Left shift- at lungs level where o2 concentration is high, there is less utilization of o2 in body.

Now you can easily solve question

1) you have doubled 2, 3 BPG - shift curve right side and cause more unloading of oxyHb. 2, 3BPG stablizes T firm of Hb ( which is not able to bind with O2)

Diseae in which high blood oxygenation and poor utilization- I have told you early that if there is no utilization than there will always high partial pressure of oxygen and curve will always be left.

2) here in this question, you have two secenario

Half BPG concentration than normal , as I told you

2,3 BPG binds to T firm of Hb and preventing it bonding from oxygen thus causing more and more unloading of oxyHb. So if you have half of BPG than normal than less unloading of Hb, more oxygen binds with Hb and this curve in presence of half amount of BPG shifts to left.

A disease in which there is mutation where 2, 3 BPG activity increaed--- more and more binding of 2, 3 BPG to HBA--- more unloading of oxygen ---- curve shift to right.

Basically curve shift to right or left depends on which allosteric modulators are present ( 2,3 BPG, increase H , decrease pH etc)

Hope this will help. For more clear just read description about various allosteric modulators.

Please post myoglobin part separately.