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19 Cards in this Set
- Front
- Back
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Globins
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Ancient soluble protein family. Hydrophobic residues are buried within interior where they stabilize the folding of the polypeptide
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Heme
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prosthetic group with planar structure. Has 4 rings; each is a pyrolle ring.
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Heme prevents spontaneous oxidation of _ to _ in presence of O2
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Fe2+ and Fe3+
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The _ structure of human hemoglobin human myoglobin, and lupine leghemoglobin are conserved.
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tertiary
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Myoglobin is a _, while hemoglobin is a _
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monomer
heterotetramer |
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proximal and distal histidines
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proximal: has an imidazole nitrogen (blue sphere) close enough to bond with iron
distale: stabilize O2 by H bonding |
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Myoglobin Oxygen saturation curve vs. hemoglobin Oxygen saturation curve
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mb: hyperbolic
hb: sigmoid |
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Torr
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a unit of pressure equal to that exerted by a column of mercury 1 mm high at 0oC and standard gravity (1 mm Hg).
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_ binding causes Fe2+ to enter the plane of the porphyrin ring
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Oxygen
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The movement of the_ on oxygenation brings the iron-associated histidine residue toward the porphyrin ring.
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iron ion
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Hill equation
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express the binding of oxygen to hemoglobin as a function of O2 concentration.
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Hill coefficient
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h, an indication of the cooperativity of O2 binding.
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The Bohr Effect
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Protons and CO2 both shift the curve to the right (weaker binding of O2).
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Lowering the pH results in
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the release of O2 from oxyhemoglobin
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Raising the CO2 partial pressure results in
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release of O2 from oxyhemoglobin
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CO2 forms a covalent bond with the_ and stabilizes the deoxy T structure.
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amino terminus of the a chain
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_ _ that stabilize the T state of hemoglobin
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Salt links
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2,3-Bisphosphoglycerate (2,3-BPG) results in
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the release of O2
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Hemoglobinopathies
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are usually classified according to the most prominent change to the protein’s structure, function or regulation.
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