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26 Cards in this Set
- Front
- Back
When a protein contains amino acid residues who interact and repell one another, what is the structure of the protein likely to be? |
A tertiary structure |
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What brand of interactions are hydrophilic interactions, hydrophobic interactions, salt bridges, hydrogen bonds, and disulfide bonds? |
Stabilizing interactions of tertiary structures |
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What interactions have an external aqueous environment pull the polar amino acid residues of a protein to the outer surface? |
Hydrophilic interactions |
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What interactions have nonpolar amino acid residues form nonpolar centers inside the protein? |
Hydrophobic interactions |
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What interactions have ionic attractions between the acidic and basic residues of amino acid residues? |
Salt bridges |
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What interactions form between the hydrogen atom of a polar residue and the oxygen or nitrogen atom of a second polar amino acid residue? |
Hydrogen bonds |
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What interactions have covalent bonds between the —SH groups of two cysteine residues? |
Disulfide bonds |
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What to the names primary, α-helix, β-pleated sheet, and triple helix indicate? |
Protein structures |
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What protein structure consists of polypeptide chains held side-by-side by H bonds? |
β-pleated sheet |
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What protein structure consists of a sequence of amino acids in a polypeptide chain? |
Primary structure |
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What protein structure consists of a corkscrew shape with H bonds between amino acids? |
α-helix |
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What protein structure consists of three peptide chains woven like a rope? |
Triple helix |
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What's the name of a protein who's spherical shape forms when polypeptide chains fold over each other? |
Globular proteins |
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What proteins are responsible for the work of cells? |
Globular proteins |
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What proteins consist of long, thin, fiber-like shapes and are involved in the structure of cells and tissues? |
Fibrous proteins |
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What do α-kerotins and β-kerotins have in common? |
They are both kinds of fibrous proteins |
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What type of fibrous protein contains three α-helices linked by disulfide bonds? |
α-keratins |
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What kind of fibrous protein contains a large amount of a β-pleated sheet structure? |
β-keratin |
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What's the name of the structure that features two or more polypeptide chains or subunits? |
Quarternary structures |
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What protein consists of two α-chains with 141 amino acids and two β-chains with 146 amino acids? |
Hemoglobin |
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What is the bodily function of hemoglobin? |
Transportation of oxygen in blood |
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What brand of stabilizing interactions are the interactions of hemoglobin identical to? |
Tertiary interactions |
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The subunits of hemoglobin consist of globular proteins. What is the name of the functional group that each of these subunits contain, capable of binding to an O molecule? |
Heme group |
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Hemoglobin and myoglobin both carry oxygen, but where does myoglobin carry oxygen in? |
In the muscles |
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Of hemoglobin and myoglobin, which one has a molar mass of 17,000 and 67,000? |
Myoglobin; hemoglobin |
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What structural levels do proteins often consist of? |
Primary, secondary, tertiary, and quarternary; all four |