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11 Cards in this Set
- Front
- Back
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What is the role of Histidine E7
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interacts with oxygen when oxygen is available
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What is the role of Valine E11
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Aids in stability of helix; holds heme in place
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What is the role of Phenylalanine CD1
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Aids in stability of helix by ensuring proper folding; holds heme in place
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What is the role of Histidine E8
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Proximal histidine that is attached to iron that pulls the complex down when oxygen binds to iron; attached to myoglobin protein
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T conformation
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deoxygenated form; tense, more stable; low affinity for oxygen (that's why so stiff); wide central channel; stabilized by ionic, hydrogen bonds
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R conformation
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relaxed, less compact, less stable form; oxygenated form of hemoglobin; narrower central channel; high affinity for oxygen binding; conformational change is due to rotational change at alpha and beta interface
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Key residues on Hb that are involved in interaction with 2,3 BPG
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His 2, lysine 82, His 143 (2 his, 1 lys), 2, 82, 143
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Hemoglobin Type A
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Normal (95% of population)
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Hemoglobin Type F
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Fetal hemoglobin; low affinity to BPG therefore increased affinity to oxygen (mutation here is histidine 146 is replaced by serine)
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Hemoglobin Type C
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hemolytic anemia--> anemic (deficiency of RBC) (mutation is instead of glycine, there is lysine; this is on helix P6 of the beta chain)
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Hemoglobin Type S
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Sickle cell trait (mutation is that instead of glycine, there is valine; @ P6, β chain)
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