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Lecture

BIOCH 200 (February 14, 2014) - Protein Structure and Function

2 Pages
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Department
Biochemistry
Course Code
BIOCH200
Professor
Walter Dixon

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BIOCH 200 (February 14, 2014) • **NOTE: The pocket in myoglobin that is available for heme group bonding is HYDROPHOBIC!!! • *Myoglobin and hemoglobin have different oxygen-binding affinities • *Kd – dissociation constant – the [L] (“L” = ligand) needed for 50% saturation to be achieved. • *Hemoglobin is a tetramer with 2 α subunits and 2 β subunits. (α subunits are identical to each other; β subunits are identical to each other)  4 polypeptides o *Therefore, hemoglobin can bind to 4 oxygen molecules o *The tertiary structures of hemoglobin and myoglobin can be super- imposed to a high degree (high homology  carrying same kind of function)  All three consist of 8 α-helices o Oxygen binding sites are invariant (is the same as in the other polypeptides)  Bind to the same helix of the polypeptide and the same histidine molecules. • *Conservative substitution: o *Amino acid substitution causes minimal protein property and conformational
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