A) contain amino acids.
B) include all the nitrogen compounds of tissues.
C) are salts of amino acids linked with one another.
D) are polymers formed by hydrogen bonding between the amino acids.
E) are polymers formed by amide linkages between the carboxyl and alpha-amino groups of alpha-amino acids.
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Multiple Choice
A) no basic amino acids
B) no acidic amino acids
C) no neutral amino acids
D) more basic than acidic amino acids
E) more acidic than basic amino acids
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Multiple Choice
A) It is found in globular proteins in both aqueous and membrane environments.
B) It may have a surface that is amphipathic (hydrophobic on one side and hydrophilic on the other) .
C) Prolines are positioned at intervals of three or four residues.
D) Side chains (R groups) pointing away from the core of the helix may stabilize its conformation.
E) There are about 3.5 amino acid residues in each turn.
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Multiple Choice
A) Addition of prosthetic groups
B) Cleavage of zymogens
C) Protein refolding after crossing a membrane
D) Stabilization of tetrameric conformation
E) Targeting to organelles
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Multiple Choice
A) Disulfide bridges.
B) Hydrophobic bonds.
C) Amide linkages between amino acid sidechains.
D) Ester linkages between sidechains of acidic and alcoholic amino acids.
E) Hydrogen bonds to water molecules.
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Multiple Choice
A) a pH values above Pi.
B) a pH values below Pi.
C) a pH value = Pi.
D) low salt concentrations.
E) none of the above
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Multiple Choice
A) ser-gly-lys-phe-lys
B) gly-lys-ser-lys-phe
C) ser-gly-lys-lys-phe
D) phe-lys-gly-ser-lys
E) ser-lys-gly-lys-phe
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Multiple Choice
A) Other than peptide bonds, hydrogen bonding is the most important interaction in pleated sheet and alpha-helical structures.
B) The peptide bond is one kind of amide linkage.
C) The native state of a protein is the least stable form under cell conditions and accordingly is easily denatured.
D) In the alpha helix, the amino acid side chains project out from the coiled backbone of the polypeptide chain.
E) Globular proteins often contain a pocket or groove into which a prosthetic group or substrate can fit.
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Multiple Choice
A) contains a sulfhydryl group
B) contains an alcoholic group
C) contains an branched chain hydrocarbon
D) doesn't have a side chain
E) contains an aromatic ring
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Multiple Choice
A) hydrogen bonds.
B) charged dipoles.
C) hydrophobic interactions.
D) disulfide bridges.
E) hydration by water.
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Multiple Choice
A) a triple helix.
B) a double alpha-helix.
C) antiparallel beta-sheet regions.
D) mostly random coil regions.
E) the lack of any stable conformation.
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Multiple Choice
A) hydrophobic interactions.
B) disulfide bonds.
C) ester bonds.
D) hydrogen bonds.
E) electrostatic interactions.
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Multiple Choice
A) contains a sulfhydryl group
B) contains an alcoholic group
C) contains an branched chain hydrocarbon
D) doesn't have a side chain
E) contains an acidic group
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Multiple Choice
A) Van Der Waals interactions.
B) peptide bonds.
C) hydrogen bonds.
D) ionic interactions.
E) hydrophobic interactions.
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Multiple Choice
A) +3
B) +2
C) +1
D) -1
E) -2
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Multiple Choice
A) lysine
B) aspartate
C) arginine
D) serine
E) glutamate
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Multiple Choice
A) glu-ala-tyr-lys
B) ser-asn-ser-ser
C) pro-gly-thr-ala
D) gly-arg-gln-trp
E) None of the other answers is correct.
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Multiple Choice
A) lysine.
B) glycine.
C) proline.
D) hydroxyproline.
E) phenylalanine.
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Multiple Choice
A) The alpha-helix conformation is stabilized by hydrophobic interactions.
B) The beta-sheet conformation is rarely found in globular proteins.
C) The folding of a polypeptide into a globular structure results in an interior enriched with hydrophobic amino acids.
D) The primary structure does not influence the native tertiary structure.
E) The subunits of proteins with quaternary structure associate through covalent bonds.
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Multiple Choice
A) planarity.
B) freedom to rotate.
C) polarity.
D) greater stability in TRANS configuration.
E) partial double bond character.
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