Myoglobin
- 77% alpha helix, 23% random coil
- eight helices: A B C D E F G H
- interior residues are non-polar (hydrophobic) except His E7 and His F8
- exterior residues are both polar and non-polar
- contains a heme cofactor:
- porphyrin ring and Fe2+
- required for protein folding and oxygen binding (oxygen binds the Fe2+)
- monomer
- high affinity for oxygen
- unaffected by pH, conc of CO2, conc of BPG
- binds 1 oxygen
- hyperbolic oxygen saturation curve
- store oxygen only
Hemoglobin
- Four subunits (tetramer):
- 2 alpha subunits (alpha globin chain)
- 2 beta subunits (beta globin chain)
- Best described as a dimer of a heterodimer
- Each alpha and beta subunits looks like myoglobin
- Main difference between Hb and Mb is due to Hb quaternary structure:
- Cooperative binding to oxygen
- Allosteric regulation by CO2, H+ and BPG
- Synthesized in RBC precursor cell: reticulocytes and erythroblasts
- Synthesis is controlled by the concentration of heme
- High proportion of alpha helix: 75% of the amino acid is associated with 8 alpha helices
- alpha helices are organized into tightly packed, nearly spherical and globular tertiery structure
- Highly soluble: polar amino acid in the exterior surface
- Each globin contains one noncovalently bound heme group
- tetramer
- moderate affinity for oxygen
- affected by pH, conc of CO2, conc of BPG
- binds 4 oxygen
- sigmoidal oxygen saturation curve
- transport oxygen (store and release)
Ok I give up. There's too much to write. Bye!
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