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23 Cards in this Set
- Front
- Back
Define:
Allosteric Interaction |
The binding of ligand at one site in a macromolecule that affects the binding of other ligands at other sites in the molecule.
See also cooperative binding |
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Define:
Bohr Effect |
The decreasing O₂ binding affinity of hemoglobin in response to a decrease in pH
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Define:
Cooperative binding |
A situation in which the binding of a ligand at one site on a macromolecule affect the affinity of other sites for the same ligand.
Both negative and positive cooperativity occur. See also allosteric interaction. |
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Define:
Heme |
A porphyrin derivative whose central Fe(II) atom is the site of reversible oxygen binding (in myoglobin and hemoglobin) or oxidation-reduction (in cytochromes).
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Define:
Hill Equation |
A mathematical expression for the degree of saturation of ligand binding to a molecule with multiple binding sites as a function of the ligand concentration.
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Define:
Hyperbolic Curve |
The graphical representation of the mathematical equation that describes the noncooperative binding of a ligand to a molecule or the rate of reaction catalyzed by a Michealis-Menten (who???) enzyme
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Define:
Ligand |
(1) A small molecule that binds to a larger molecule.
(2) A molecule or ion bound to a metal ion. |
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Microfilament |
A 70-Å-diameter cytoskeletal element composed of actin.
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Define:
Myofibril |
The bundle of fibers that are arranged in register in striated muscle cells
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Define:
Noncooperative binding |
A situation in which binding of a ligand to a macromolecule does not affect the affinities of other binding sites oin the same molecule.
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Define:
Oxygenation |
The binding of molecular oxygen, e.g. to a heme group
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Define:
P₅₀ |
For a gaseous ligand, the ligand concentration, in units of pressure (e.g. torr), at which a binding protein such as hemoglobin is half-saturated with ligand.
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Define:
pO₂ |
Partial oxygen pressure
The concentration of gaseous O₂ in units of pressure (e.g. torr) |
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Define:
R State |
One of two conformations of an allosteric protein; the other is the T state. The R state is usually the catalytically more active state.
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Define:
Sarcomere |
The repeating unit of a myofibril, consisting of thin and thick filaments that slide past each other during muscle contraction.
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Define:
Saturation |
The state in which all of a macromolecule's ligand-binding sites are occupied by a ligand.
See also enzyme saturation and saturated fatty acid. |
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Define:
Sigmoidal curve |
The S-shaped graphical representation of the cooperative binding of a ligand to a molecule.
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Define:
Sliding Filament Model |
A mechanism for muscle contraction in which interdigitated thin and thick filaments move past each other so as to shorten the overall length of a sarcomere.
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Define:
Striated Muscle |
The voluntary or skeletal muscles, which have a striped microscopic appearance.
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T State |
One of two conformations of an allosteric protein; the other is the R state. The T state is usually the catalytically less active state.
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Define:
Thick filament |
The sarcomere element that is composed primarily of several hundred myosin molecules
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Define:
Thin filament |
The sarcomere element that is composed primarily of actin, along with tropomyosin and troponin.
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Define:
Yo₂ |
Fractional Saturation (Y)
The fraction of a protein's ligand-binding sites that are occupied by ligand. For example, Yo₂ is the fractional saturation of a protein's oxygen-binding sites. |