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content/Biokemi/Hemoglobin/Instuderingsfrågor.md

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+#### Describe L1/2 in terms of receptor and ligand binding.
+
+$L_{1/2}$ is the amount of L needed to reach 50%/balance of ligand/receptor. The value can be different depending on the binding affinity, how strong the ligand/receptor binds to each other
+#### Explain the basic structure of myoglobin including the porphyrin ring and Fe.
+Myoglobin består av en polypeptidkedja med heme som en prostetisk grupp. Heme består av en porfyrinring som är fyra pyrroleringar och en järnatom i mitten som kan binda syre. 
+#### What are proximal and distal histidine? How do they interact with heme molecule?
+
+Den proximal binder direkt till 
+#### How does $O^2$ bind to myoglobin? Compare with carbon monoxide ($CO$).
+
+Den binder till järn den distala histidinen. CO binder bara till järn
+#### Explain the basic structure of hemoglobin and its structural states.
+#### What is cooperative binding? Describe in the context of hemoglobin.
+#### Compare the dissociation curves of myoglobin and hemoglobin. What does this mean for the transport of O2 from the lungs to the tissues?
+#### Define an allosteric regulator.
+#### How is hemoglobin affected by CO, CO2, H+, and 2,3-BPG? How are these effects mediated? Where do these molecules/ions bind and what are the consequences?
+#### Define Bohr effect and explain how it influences oxygen binding.
+Bohr-effekten är hur vätejoner och 2,3-BPGs koncentrationer ändrar bindningsaffiniteten för syre i Hb, i lugnorna är det lägre där binder syre bättre än  där det ska frisläppas som har högre koncentration av vätejoner/2,3-BPG.
+#### How does fetal hemoglobin (HbF) differ from adult hemoglobin (HbA) and what effect does this have?
+#### Explain the molecular and structural background of sickle-cell disease.