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Why is silk fibroin so strong,but at the same time so soft and flexible?

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Unlike collagen and keratin,silk fibroin...

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Experiments on denaturation and renaturation after the reduction and reoxidation of the -S-S- bonds in the enzyme ribonuclease (RNase) have shown that:


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.

F) B) and C)
G) A) and C)

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Which of the following is not an appropriate description for van der Waals interactions?


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.

F) A) and D)
G) C) and D)

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Proteins often have regions that can fold and function as an independent entity from the whole protein.These regions are called:


A) domains.
B) oligomers.
C) peptides.
D) sites.
E) subunits.

F) C) and D)
G) A) and B)

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Describe three of the important features of a β\beta sheet polypeptide structure.Provide one or two sentences for each feature.

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In the blured image sheet structure,several extended...

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An average protein will not be denatured by:


A) a detergent such as sodium dodecyl sulfate.
B) heating to 90°C.
C) iodoacetic acid.
D) pH 10.
E) urea.

F) B) and E)
G) A) and C)

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Thr and/or Leu residues tend to disrupt an α\alpha helix when they occur next to each other in a protein because:


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.

F) A) and C)
G) B) and C)

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Describe a reservation about the use of x-ray crystallography in determining the three-dimensional structures of biological molecules.

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To obtain an x-ray picture of a biomolec...

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A sequence of amino acids in a certain protein is found to be -Ser-Gly-Pro-Gly-.The sequence is most probably part of a(n) :


A) antiparallel β\beta sheet.
B) parallel β\beta sheet.
C) ( α\alpha helix.)
D) ( α\alpha sheet.)
E) ( β\beta turn.)

F) B) and D)
G) None of the above

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Which of the following statements concerning the process of spontaneous folding of proteins is false?


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.

F) C) and D)
G) All of the above

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Which of the following statements concerning protein domains is true?


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.

F) B) and E)
G) B) and D)

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Each of the following reagents or conditions will denature a protein.For each,describe in one or two sentences what the reagent/condition does to destroy native protein structure. (a)urea (b)high temperature (c)detergent (d)low pH

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(a)Urea acts primarily by disrupting hyd...

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What is typically found in the interior of a water-soluble globular protein?

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Hydrophobic amino acid residues cluster ...

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An α\alpha helix would be destabilized most by:


A) an electric dipole spanning several peptide bonds throughout the α\alpha 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 α\alpha helix.
E) the presence of two Lys residues near the amino terminus of the α\alpha helix.

F) B) and C)
G) B) and D)

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Explain (succinctly)the theoretical and/or experimental arguments in support of this statement: "The primary sequence of a protein determines its three-dimensional shape and thus its function."

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Anfinsen showed that a complet...

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Pauling and Corey's studies of the peptide bond showed that:


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.

F) None of the above
G) C) and E)

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In superhelical proteins,such as collagen,several polypeptide helices are intertwined.What is the function of this superhelical twisting?

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The superhelical twisting of m...

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Any given protein is characterized by a unique amino acid sequence (primary structure)and three-dimensional (tertiary)structure.How are these related?

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The three-dimensional structure is deter...

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How can changes in pH alter the conformation of a protein?

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Changes in pH can influence the extent t...

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What are two mechanisms by which "chaperone" proteins assist in the correct folding of polypeptides?

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Chaperones protect unfolded po...

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