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(Haemoglobin) - Coggle Diagram
Haemoglobin
STATE
relaxed
Oxyhemoglobin state
where O2 binding moves the iron atom into the porphyrin plane, rupturing salt bridges between dimers
produce a high O2 affinity conformation
Taut
Deoxyhemoglobin state
strong ionic salt bridges and hydrogen bonds between alpha-beta dimers (stronger interaction)
resulting in low O2 affinity
State, based on interactions of dimers
(Alpha1Beta1 interecating with (Alpha2Beta)
within dimer strong hydrophobic forces
between dimer forces are weak ionic and hydrogen bonds
Interaction is broken by binding of O2
Comparison
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Curve
STRUCTURE
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