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15 Cards in this Set
- Front
- Back
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oligomer
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proteins with more than one subunit
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protomer
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consists of one pp chain or several unlike pp chains
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What is considered a protein's quaternary structure?
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the spatial arrangement of a macromolecule's individual subunits
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What is the only type of symmetry that proteins can have?
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rotational
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What is hydropathy?
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the combined hydrophobic and hydrophilic tendencies of individual amino acid residues in proteins
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A larger hydropathy makes what more likely?
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for the residue to occupy the interior of the proein
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T/F
Hydrogen bonds make only minor contributions to protein stability. |
T
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For what are H-bonds important in proteins (considering quaternary structure)
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important determinants of native structure
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ion pair/ salt bridge
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association of 2 ionic protein groups of opposite charge
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Why is Zinc ideal for the structural role in intracellular proteins?
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-its filled d electron shell permits it to interact strongly with a variety of ligands (sulfur, nitrogen, oxygen)
-has only one stable oxidation state and so does not undergo oxidation-reduction in the cell |
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What is a ligand?
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1. a small molecule that binds to a larger one
2. a molecule or ion bound to a metal ion |
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In what geometry are Zinc fingers coordinated?
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tetrahedral
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What is breathing?
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the small conformational fluctuations of a protein molecule
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What are chaotropic agents?
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ions or small organic molecules that increase the solubility of nonpolar substances in water
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What did Anfinsen's work on ribonuclease A (RNase A) show?
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proteins can fold spontaneously into their native conformations under physiological conditions---- A PROTEIN'S PRIMARY STRUCTURE DICTATES ITS 3-D STRUCTURE
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