A) altering net charge by changing pH
B) changing the salt concentration
C) disruption of weak interactions by boiling
D) exposure to detergents
E) mixing with organic solvents such as acetone
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A) proteins are synthesized.
B) proteins are folded.
C) proteins are modified.
D) proteins are degraded.
E) protein levels are maintained.
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A) are roughly parallel to the axis of the helix.
B) are roughly perpendicular to the axis of the helix.
C) occur mainly between electronegative atoms of the R groups.
D) occur only between some of the amino acids of the helix.
E) occur only near the amino and carboxyl termini of the helix.
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A) alternate between the outside and the inside of the helix.
B) are found on the outside of the helix spiral.
C) cause only right-handed helices to form.
D) generate the hydrogen bonds that form the helix.
E) stack within the interior of the helix.
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A) All of them
B) II, III, and IV
C) I, II, and IV
D) I, II, and III
E) I and IV
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A) at pH 7, many different peptide bond conformations are equally probable.
B) peptide bonds are essentially planar, with no rotation about the C-N axis.
C) peptide bonds in proteins are unusual, and unlike those in small model compounds.
D) peptide bond structure is extraordinarily complex.
E) primary structure of all proteins is similar, although the secondary and tertiary structure may differ greatly.
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A) entropy increase from the decrease in ordered water molecules forming a solvent shell around it.
B) maximum entropy increase from ionic interactions between the ionized amino acids in a protein.
C) sum of free energies of formation of many weak interactions among the hundreds of amino acids in a protein.
D) sum of free energies of formation of many weak interactions between its polar amino acids and surrounding water.
E) stabilizing effect of hydrogen bonding between the carbonyl group of one peptide bond and the amino group of another.
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A) They are a form of secondary structure.
B) They are examples of structural motifs.
C) They consist of separate polypeptide chains (subunits) .
D) They have been found only in prokaryotic proteins.
E) They may retain their correct shape even when separated from the rest of the protein.
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A) in the interior of a protein of a bacterium that lives in humans.
B) on the exterior of a protein of a bacterium that lives in humans.
C) in the interior of a protein of a thermophilic archaeal organism.
D) on the exterior of a protein of a thermophilic archaeal organism.
E) A salt bridge would be equally likely to be found in any of these cases.
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A) macromolecular
B) fibrous
C) globular
D) helical
E) membrane
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A) parallel sheet.
B) antiparallel sheet.
C) right-handed helix.
D) left-handed helix.
E) turn.
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A) always side by side.
B) generally near each other in sequence.
C) invariably restricted to about 7 of the 20 standard amino acids.
D) often on different polypeptide strands.
E) usually near the polypeptide chain's amino terminus or carboxyl terminus.
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A) 1
B) 2.8
C) 3.6
D) 4.2
E) 10
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A) I
B) II
C) III
D) IV
E) None of the answers is correct.
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A) amino-acid sequence.
B) evolutionary relationships.
C) function.
D) secondary structure content and arrangement.
E) subunit content and arrangement.
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