Test Bank for Biochemistry, 4th Edition : Garrett Grisham

Test Bank for Biochemistry, 4th Edition : Garrett

Grisham

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Name Chapter 6--Proteins: Secondary, Tertiary, and Quaternary Structure

Description
Instructions

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Multiple Choice

Question Amino acid side chains capable of forming hydrogen bonds are usually located
on the protein ____ and form hydrogen bonds primarily with the ____.
Answer surface, water solvent
interior, water solvent
surface, other amino acid side chains
interior, other amino acid side chains
all are true

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Multiple Choice

Question ____ amino acids are almost never found in the interior of a protein, but the
protein surface may consist of ____ amino acids.
Answer Nonpolar, both polar and nonpolar
Nonpolar, mostly nonpolar
Polar, both polar and nonpolar
Polar, only polar
Polar, only nonpolar

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Multiple Choice

Question Electrostatic interactions among amino acid residues on proteins may be

damped out by high concentrations of:
Answer water.
organic solvents.
salts.
heat.
all of the above.

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Multiple Choice

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Question An electrostatic interaction might occur within a protein between which of the
following amino acid pairs at typical physiological pH?
Answer Ser/Asn
Asp/Glu
Arg/Cys
Lys/Asp
Val/Ile

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Multiple Choice

Question ____ between tightly packed amino acid side chains in the interior of the protein
are a major contribution to protein structure.
Answer Hydrogen bonds
Electrostatic interactions
Covalent ester bonds
Van der Waals interactions
All are true

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Multiple Choice

Question A hydrophobic interaction might occur within a protein between which of the
following amino acid pairs?
Answer Ser/Ile
Val/Leu
Tyr/Cys
Lys/Asn
His/Val

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Multiple Choice

Question All of the information necessary for folding the peptide chain into its "native"
structure is contained in the ____ of the peptide.
Answer amino acid sequence
amino acid composition
configuration
amino acid side chain charges
all are true

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Multiple Choice

Question Amino acid sequence is:

Answer primary structure.
secondary structure.
tertiary structure.
quaternary structure.

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regular structure.

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Multiple Choice

Question Secondary and higher orders of structure are determined by all EXCEPT:
Answer hydrophobic interactions.
ionic bonds.
van der Waals forces.
hydrogen bonds.
peptide bonds.

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Multiple Choice

Question The resonance structure which forms the "amide plane" contains which atoms?
Answer Ca H-NH-CO-C-CaH
Ca H-NH-CO
Ca -NH-CO-Ca
NH-CO
NH-CO-Ca

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Multiple Choice

Question Planarity of the peptide bond means that rotation is allowed about the bond linking
the ____ and the carbon of the peptide bond, and also about the bond linking the ____ to
the adjacent a-carbon.
Answer a-carbon, carbonyl carbon
b-carbon, carbonyl carbon
carbonyl carbon, nitrogen of the peptide bond
a-carbon, nitrogen of the peptide bond
none are true

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Multiple Choice

Question A Ramachandran plot shows:

Answer the amino acid residues which have the greatest degree of rotational freedom.
the sterically allowed rotational angles between R groups and a-carbons in a
peptide.
the sterically allowed rotational angles between Ca and the amide nitrogen
(Ca-N) as well as between Ca and the amide carbonyl carbon (Ca -CO).
the sterically allowed rotational angles about the amide nitrogen (NH) and CO.
the amino acid residues that form a-helix, b-sheet, etc.

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Multiple Choice

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Question Alpha helices are stabilized primarily by:

Answer hydrogen bonds between the main chain peptide bond component atoms.
electrostatic interactions between R-groups.
hydrophobic interactions between the a-carbons of the main chain.
hydrogen bonding between the R-groups.
hydrophobic interactions between R-groups and the solvent water.

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Multiple Choice

Question In the majority of a-helixes, each peptide carbonyl is hydrogen bonded to the
peptide N-H group ____ residues farther ____ the chain.
Answer 2, down
4, up
3, down
2, up
4, down

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Multiple Choice

Question ____ and ____ act as helix breakers due to their unique structure, which fixes the
value of the Ca -N-C bond angle.
Answer Histidine, lysine
Proline, hydroxyproline
Arginine, lysine
Serine, threonine
Tyrosine, serine

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Multiple Choice

Question If the following section of a polypeptide is folded into an a-helix, to which amino
acid is the carbonyl group of alanine hydrogen bonded?

ala-ser-val-asp-glu-leu-gly
Answer serine
aspartic acid
glutamic acid
leucine
valine

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Multiple Choice

Question When the peptide (AEFFLAMEP) forms an a-helix, which amino acid residue
would be closest to being in the same position on the same face of the helix as is the initial
alanine residue?

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Answer F(3)
A(6)
E(8)
P(9)
L(5)

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Multiple Choice

Question Antiparallel b-sheets have:

Answer sheets that progress from N to C termini in the same direction.
usually all of their hydrophobic residues on one side of the sheet.
all hydrophobic residues.
all hydrophilic residues.
fibers that can be stretched or extended, but are not flexible.

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Multiple Choice

Question b-Turns in a peptide chain form a tight loop with hydrogen bonding of the carbonyl
oxygen with:
Answer side chain amine of lysine two amino acids down the chain.
amide proton on the next amino acid down the chain.
amide proton of the glutamine side chain.
amide proton of the residue three positions down the chain.
amide proton of asparagine side chain.

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Multiple Choice

Question Polylysine is a random coil when the pH is less than 11, while it forms an a-helix if
the pH is raised to greater than 12. This is because at pH 12:
Answer the lysine residues are negatively charged which electrostatically stabilizes the
helix.
the positive charges on the lysine residues stabilizes the a-helix.
the lysine residues are neutral which eliminates electrostatic repulsion
between the R groups.
the high concentration of OH- ions in solution reduces the electrostatic
repulsion between the R-groups.
the lysine side chain changes configuration with pH.

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Multiple Choice

Question The amino acid residue most likely to be found in a beta turn is:
Answer glycine.
alanine.
valine.
glutamic acid.

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leucine.

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Multiple Choice

Question ____ b-sheets characteristically distribute hydrophobic side chains on both sides
of the sheet, and ____b-sheets are usually arranged with all their hydrophobic residues on
one side of the sheet.
Answer Antiparallel, parallel
Antiparallel, antiparallel
Parallel, antiparallel
Parallel, parallel
None of the above

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Multiple Choice

Question ____ form between two normal b-structure hydrogen bonds and are comprised
of two residues on one strand and one residue on the opposite strand.
Answer a-Helix
Parallel b-sheet
b-Turn
b-Bulge
a-Turn

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Multiple Choice

Question Tertiary structure is defined as:

Answer the sequence of amino acids.
the folding of a single polypeptide chain in three-dimensional space.
hydrogen bonding interactions between adjacent amino acid residues into
helical or pleated segments.
the way in which separate folded monomeric protein subunits associate to form
oligomeric proteins.
all are true.

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Multiple Choice

Question Tertiary structure of proteins depends on all EXCEPT:

Answer protein structure depends on primary structure.
a-helices and b-sheets often associate and pack close together.
secondary structures form whenever possible.
proteins are stable as a single-layer structure.
peptide segments between secondary structures are short.

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Multiple Choice

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Question The "Greek Key" topology is composed of ____.

Answer Adjacent a-helices oriented in the same direction
Adjacent a-helices oriented in the opposite direction
Discreet regions of b-sheet oriented in an antiparallel fashion
Discreet regions of b-sheet oriented in an antiparallel fashion
Parallel b-sheet structures connected by a-helices

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Multiple Choice

Question Fibrous proteins contain polypeptide chains ____ producing long fibers or large
sheets.
Answer with an abundance of aromatic amino acids
with an abundance of hydrophilic amino acids
organized approximately parallel along a single axis
with amino acids arranged in a repeating (-a-b-c-d-)n sequence
all are true

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Multiple Choice

Question a-Keratin has all of the following characteristics EXCEPT:

Answer primary component in hair, claws, fingernails, and horns of animals.
consists of four helical strands arranged as twisted pairs of two-stranded coiled
coils.
has associated hydrophobic strips on the two coiled coils.
principal constituent of connective tissues in animals.
has covalent disulfide bonds to stabilize the structure.

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Multiple Choice

Question The "permanent" part of adding wave in hair is primarily due to:
Answer rearrangement of hydrogen bonds between hair fibers.
reestablishment of new ionic interactions between hair fibers.
breaking and reforming peptide bonds in the hair polypeptides.
rearrangement of hydrophobic interactions in hair fibers.
reduction and re-oxidation of disulfide bonds in hair fibers.

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Multiple Choice

Question Silk fibers consist of ____ proteins consisting of alternating ____ and ____ or
____ residues.
Answer fibroin; glycine; proline; leucine
a-keratin; alanine; glycine; serine
fibroin; glycine; alanine; threonine
b-keratin; cysteine; alanine; proline
fibroin; glycine; alanine; serine

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Multiple Choice

Question Collagen has the following characteristics EXCEPT:

Answer Tropocollagen is the basic structural unit.
There is about 33% glycine in collagen.
Both intermolecular and intramolecular crosslinks help to stabilize the collagen
fibrils.
Modification of prolines occurs prior to collagen synthesis.
Inextendable fibrous protein are components of connective tissues.

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Multiple Choice

Question The unique composition of collagen is accommodated in a structure called a(n):

Answer b-pleated sheet.
triple helix.
helix-turn-helix motif.
coiled coils.
all are true.

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Multiple Choice

Question Prolyl hydroxylase has all of the following characteristics EXCEPT:

Answer requires citric acid.
is activated by Fe2+.
hydroxylates proline residues in proteins.
requires molecular oxygen.
requires a-ketoglutarate.

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Multiple Choice

Question A major stabilizing factor in the triple helix is a ____ structure such that ____
residues from the three strands stack along the center of the triple helix.
Answer linear, glu
linear, gly
staggered, lys
staggered, gly
stacked, pro

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Multiple Choice

Question In hemoglobin, a ____ protein, the space between the helices is filled efficiently
and tightly with mostly ____ amino acid chains and with ____ side chains facing the outside
of the protein structure.

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Answer globular, hydrophobic, polar

globular, polar, nonpolar
fibrous, hydrophobic, nonpolar
fibrous, polar, nonpolar
none are true

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Multiple Choice

Question Why should the core of most globular and membrane proteins consist almost
entirely of a-helix and b-sheets?
Answer Hydrogen bonded structures must be kept away from water solvent.
Highly polar N-H and C=O moieties of the peptide backbone must be
neutralized in the hydrophobic core of the protein.
Hydrogen bonding only occurs in the core of proteins.
Trapped water stabilizes the helix and sheet structures.
None are true.

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Multiple Choice

Question The outward face of a(n) ____ consists mainly of polar and charged residues,
whereas the inner face contains mostly nonpolar, hydrophobic residues.
Answer b-sheet
configuration
b-turn
amphiphilic helix
all are true

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Multiple Choice

Question A b-barrel would most likely be composed of ____.

Answer parallel b-sheets connected by regions of a-helix
parallel b-sheets connected by b-turns.
parallel b-sheets connected by regions of random coil.
parallel b-sheets connected disulfide bonds.
both a and c are correct.

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Multiple Choice

Question Flexible, disordered segments of proteins are commonly high in the amino acid:
Answer leu
lys
ser
pro
asp

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Multiple Choice

Question All are true for collective motions of proteins EXCEPT:

Answer are movements of groups of atoms covalently linked in such a way that the
group moves as a unit.
include trypsin ring flips
include cis-trans isomerization of prolines.
involve the flexible antigen-binding domains of immunoglobulins.
all are true.

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Multiple Choice

Question Which statement is correct about the b-a-b motif?

Answer The two b-strands are antiparellel.
The peptide segment connecting the b-strands usually contains no more than
five amino acids.
The peptide segment connecting the two b-strands commonly contains proline.
The cross-over connection itself contains an a-helical segment.
none are correct.

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Multiple Choice

Question All are true about the tertiary structure of the enzyme triose phosphate isomerase
EXCEPT:
Answer Its b-strands are parallel.
Its a-helices are in the interior of the molecular structure.
It contains a b-barrel in the center of its structure.
It is composed entirely of alternating a-helices and b-strands.
All are true.

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Multiple Choice

Question All are classes of globular proteins according to type and arrangement of
secondary structure EXCEPT:
Answer small metal- and disulfide-rich proteins.
parallel or mixed b-sheet.
antiparallel b-sheet.
antiparallel a-helix.
all are true.

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Multiple Choice

Question ____ are examples of antiparallel a-helix proteins.

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Answer Triose phosphate isomerase

Pyruvate kinase
Flavodoxin
Hemoglobin
Papain

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Multiple Choice

Question ____ is an example of a disulfide-rich protein.

Answer Insulin
Glyceraldehydes-3-phosphate dehydrogenase
Hemoglobin
Triose phosphate isomerase
All are true.

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Multiple Choice

Question ____ are proteins that help other proteins to fold.

Answer Immunoglobulins
Phospholipases
Synthetases
Molecular chaperones
Proteases

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Multiple Choice

Question All are structural and functional advantages to quaternary structure EXCEPT:
Answer cooperativity.
stability.
bringing catalytic sites together.
genetic economy and efficiency.
all are true.

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Multiple Choice

Question All of the statements about the tertiary structure of the enzyme triose phosphate
isomerase are correct EXCEPT:
Answer Its b-strands are parallel.
Its a-helices are in the interior core of the molecular structure.
It contains a b-barrel in the center of its structure.
It is composed entirely of alternating a-helices and b-strands.
Hydrophobic residues are buried between concentric layers.

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Test Bank for Biochemistry, 4th Edition : Garrett Grisham

Multiple Choice

Question Arrange the steps involved in folding of globular proteins into a proper sequence.

A. "Molten globule" formation of assembled domains.

B. Formation of domains through cooperative aggregation of folding nuclei.
C. Adjustment in the conformation of domains.
D. Rapid and reversible formation of local secondary structure.
E. Final protein monomer formation.
Answer A, B, C, D, E
B, C, E, A, D
D, C, B, A, E
D, B, A, C, E
B, D, C, A, E

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