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9. Hemoglobin/Allosterism
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06/03/2024
important characteristics of M-M behavior vs cooperative binding behavior (hemoglobin)
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myoglobin vs hemoglobin kinetics
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cooperativity is measured by the ...
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resting level of O2 consumption
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Explain via the Fick Equation why hypothetical myoglobin-loaded erythrocytes could not reasonably supply the resting level of oxygen consumption (250 …
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difference between myoglobin/hemoglobin structures
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Describe how heme-initiated structural remodeling at the oligmeric interface occurs. (both O2 side and 2,3-BPG side) ALLOSTERIC REGULATION
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Describe how hemoglobin's inter-subunit salt-bridges are affected by the conformational transition from T-state to R-state.
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describe the 'stickiness' of hemoglobin as it relates to O2 saturation (I am making up this term. Not Dr. King's)
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which state of hemoglobin is more favored (T/R)
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mechanism by which 2,3-BPG regulate hemoglobin
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describe the mechanism by which increased pH stabilizes T-state hemoglobin
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Describe the mechanism by which CO2 stabilizes T-state hemoglobin and why this is desirable/important.
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Define the Bohr Effect
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Define the Haldane Effect:
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Describe the key characteristics of thalassemia.
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Describe the key characteristics of sickle cell anemia
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Describe the key characteristics methemoglobinemia.
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Describe the diagnostic uses of hemoglobin in FMRI
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Describe the diagnostic uses of hemoglobin in HbA1c
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Describe the diagnostic uses of hemoglobin in pulse-oximetry
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