305362
Beschreibung
Mindmap von kathrynmoar, aktualisiert more than 1 year ago
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Erstellt von kathrynmoar
vor mehr als 10 Jahre
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Hemoglobin
- Structure
- tetramer, made up of two alpha
subunits and two beta subunits.
each binds a heme
- subunit has similar
structure to myoglobin
- tetramer, made up of two alpha
subunits and two beta subunits.
each binds a heme
- Myoglobin
- made up of alpha helices with connecting
loops with heme sitting in a pocket
- Heme contains iron which
can bind to oxygen at one of
its six ligand sites
- only unloads oxygen when levels become
unusually low.
- made up of alpha helices with connecting
loops with heme sitting in a pocket
- Binding of Oxygen
- four oxygen molecules bind per
hemoglobin, one per subunit.
- binding curve = sigmodial
- binding of one oxygen molecule makes it
easier for a second to bind
- homotrophic positive cooperative effect =
affinity of binding of oxygen for the fourth
oxygen is 20 fold greater than the affinity for
the first oxygen
- binding of one oxygen molecule makes it
easier for a second to bind
- four oxygen molecules bind per
hemoglobin, one per subunit.
- Allosteric change
- alpha and beta subunit are more
associated with each other than the other
two subunits
- when oxgen binds, the subunits change their position. this is due
to the change of shape of heme when oxygen binds.
- When oxygen isnt bound iron doesnt fit in the
planar structure but when bound it becomes
smaller and can fit
- When oxygen isnt bound iron doesnt fit in the
planar structure but when bound it becomes
smaller and can fit
- when oxgen binds, the subunits change their position. this is due
to the change of shape of heme when oxygen binds.
- this change results in the molecule shifting
from low affinity (T) to high affinity (R) state.
- alpha and beta subunit are more
associated with each other than the other
two subunits
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