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Which factor is LEAST likely to result in protein denaturation?


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

F) All of the above
G) A) and B)

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Proteostasis is the cellular process by which:


A) proteins are synthesized.
B) proteins are folded.
C) proteins are modified.
D) proteins are degraded.
E) protein levels are maintained.

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

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In the α\alpha helix, the hydrogen bonds:


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.

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

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Name four factors (bonds or other forces) that contribute to stabilizing the native structure of a protein, and describe one condition or reagent that interferes with each type of stabilizing force.

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1. Hydrophobic interactions: Hydrophobic...

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In an α\alpha helix, the R groups on the amino acid residues:


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.

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

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Of the following bonds, which have freedom of rotation? I. N - C α\alpha II) C α\alpha - C III) C - N IV) R - C α\alpha


A) All of them
B) II, III, and IV
C) I, II, and IV
D) I, II, and III
E) I and IV

F) A) and B)
G) A) 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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One reservation about the use of x-ray c...

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

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Pauling and Corey showed that in small peptides, six atoms associated with the peptide bond all lie in a plane. On a dipeptide of two amino acids in trans linkage (side-chains can be shown as -R), which six atoms are part of the planar structure of the peptide bond?

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In a dipeptide consisting of two amino a...

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The MOST important contribution to the stability of a protein's conformation appears to be the:


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.

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

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Which statement 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) A) and D)
G) A) and B)

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A salt bridge would be MOST likely to be found:


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.

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

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A _____ protein will often have properties that allow it to be both strong and flexible.


A) macromolecular
B) fibrous
C) globular
D) helical
E) membrane

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

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The secondary structure shown below is an example of a(n) :  The secondary structure shown below is an example of a(n) :   A)  parallel  \beta  sheet. B)  antiparallel  \beta  sheet. C)  right-handed  \alpha  helix. D)  left-handed  \alpha  helix. E)   \beta  turn.


A) parallel β\beta sheet.
B) antiparallel β\beta sheet.
C) right-handed α\alpha helix.
D) left-handed α\alpha helix.
E) β\beta turn.

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

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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 primary structure of a protein refer...

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Explain what is meant by motifs in protein structure.

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Motifs in protein structure refer to spe...

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The three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are:


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.

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

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Roughly how many amino acids are there in one turn of an α\alpha helix?


A) 1
B) 2.8
C) 3.6
D) 4.2
E) 10

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

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Which image below shows that there are folding intermediates with substantial stability along nearly every folding pathway? Which image below shows that there are folding intermediates with substantial stability along nearly every folding pathway?   A)  I B)  II C)  III D)  IV E)  None of the answers is correct.


A) I
B) II
C) III
D) IV
E) None of the answers is correct.

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

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The structural classification of proteins (based on motifs) is based primarily on their:


A) amino-acid sequence.
B) evolutionary relationships.
C) function.
D) secondary structure content and arrangement.
E) subunit content and arrangement.

F) C) and D)
G) C) and E)

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