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A) folding of denatured RNase into the native,active conformation,requires the input of energy in the form of heat.
B) native ribonuclease does not have a unique secondary and tertiary structure.
C) the completely unfolded enzyme,with all -S-S- bonds broken,is still enzymatically active.
D) the enzyme,dissolved in water,is thermodynamically stable relative to the mixture of amino acids whose residues are contained in RNase.
E) the primary sequence of RNase is sufficient to determine its specific secondary and tertiary structure.
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A) They involve dipole-dipole interactions.
B) Their strength depends on the distance between the two interacting atoms.
C) They are highly specific.
D) An individual van der Waals interaction does not contribute significantly to the stability of a protein.
E) They can involve hydrophobic amino acids.
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A) domains.
B) oligomers.
C) peptides.
D) sites.
E) subunits.
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A) a detergent such as sodium dodecyl sulfate.
B) heating to 90°C.
C) iodoacetic acid.
D) pH 10.
E) urea.
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A) an amino acids like Thr is highly hydrophobic.
B) covalent interactions may occur between the Thr side chains.
C) electrostatic repulsion occurs between the Thr side chains.
D) steric hindrance occurs between the bulky Thr side chains.
E) the R group of Thr can form a hydrogen bond.
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A) antiparallel sheet.
B) parallel sheet.
C) ( helix.)
D) ( sheet.)
E) ( turn.)
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A) It may be an essentially random process.
B) It may be defective in some human diseases.
C) It may involve a gradually decreasing range of conformational species.
D) It may involve initial formation of a highly compact state.
E) It may involve initial formation of local secondary structure.
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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) an electric dipole spanning several peptide bonds throughout the helix.
B) interactions between neighboring Asp and Arg residues.
C) interactions between two adjacent hydrophobic Val residues.
D) the presence of an Arg residue near the carboxyl terminus of the helix.
E) the presence of two Lys residues near the amino terminus of the helix.
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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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