Chem 221 - Biochemistry for Science Majors » Fall 2021 » L6 3D Structure of Proteins Part 2 of 2
Need help with your exam preparation?
Get Answers to this exam for $6 USD.
Get Answers to all exams in [ Chem 221 - Biochemistry for Science Majors ] course for $25 USD.
Existing Quiz Clients Login here
Question #1
Ala and Leu are strong alpha-helix breakers.
A.
TRUE
B.
FALSE
Question #2
Glycine is often found in the middle of an alpha-helix.
A.
TRUE
B.
FALSE
Question #3
In the α-helix structure, the protein backbone is wound around an imaginary axis, and the R groups of the amino acid residues run parallel the axis.
A.
FALSE
B.
TRUE
Question #4
The pitch of a helix is 3.6 angstroms.
A.
FALSE
B.
TRUE
Question #5
Within an α helix, each carbonyl oxygen (residue n) of the polypeptide backbone is hydrogen-bonded to the backbone amide hydrogen of the fifth residue further toward the C-terminus.
A.
FALSE
B.
TRUE
Question #6
Each hydrogen bond in a alpha helix closes a loop containing 3.6 atoms.
A.
FALSE
B.
TRUE
Question #7
The stability of an alpha-helix is affected by the side and the identity of the side chains.
A.
TRUE
B.
FALSE
Question #8
Because of the geometry of the individual amino acids, the hydrogen bonds of an antiparallel beta sheet occur at an angle.
A.
FALSE
B.
TRUE
Question #9
Ala and Leu are strong a-helix formers.
A.
TRUE
B.
FALSE
Question #10
Antiparallel beta sheets are more stable than parallel beta sheets.
A.
FALSE
B.
TRUE
Question #11
The side chains of a beta sheet are oriented parallel to the plane of the sheet.
A.
TRUE
B.
FALSE
Question #12
Collagen, the most abundant protein in the body, is an example of what type of protein?
A.
Fibrous
B.
Peripheral
C.
Globular
D.
Integral
Question #13
β turns connect the ends of two adjacent segments of a parallel β sheet.
A.
FALSE
B.
TRUE
Question #14
Which of the following is an example of the secondary structure of a protein?
A.
Hydrophobic interactions
B.
Hydrogen bonding between an amine and carbonyl group
C.
Peptide bonding between amino acids
D.
Disulfide bonds between cysteine residues
E.
Hydrogen bonding between R groups
Question #15
What does the quaternary structure of a protein involve?
A.
partial denaturation
B.
the association of two or more peptide chains
C.
random coil alternating with a-helix
D.
the complete three-dimensional conformation
Question #16
What kinds of interactions do NOT contribute to the tertiary protein structure?
A.
disulfide bridges
B.
Van der Waals interactions
C.
hydrogen bonds
D.
peptide bonds
E.
salt bridges
Question #17
Which of the following properties of a protein is least likely to be affected by changes in pH?
A.
Tertiary structure
B.
Net charge
C.
Secondary structure
D.
Primary structure
Question #18
A structure that has hydrogen bonds between polypeptide chains arranged side by side is
A.
tertiary structure
B.
alpha helix
C.
primary structure
D.
beta sheet
Question #19
The term "denaturation," when used in conjunction with proteins or nucleic acids, refers to a change in structural characteristics primarily due to __________.
A.
changes in primary structure
B.
the disruption of non-covalent bonds
C.
the binding of toxic compounds
D.
the disruption of covalent bonds
Question #20
Disulfide bonds in a protein chain connect ________.
A.
an amine and a carboxylic acid group
B.
two asparagine residues
C.
two cysteine residues
D.
tryptophan and alanine residues
E.
an alcohol and a carboxylic acid group
Question #21
In the β-pleated sheet secondary structure of a protein, two or more amino acid sequences in separate parts of the protein are held together ________.
A.
by hydrogen bonding between different sections of the polypeptide chain
B.
in random order, due to hydrophobic interactions
C.
in a triple helix
D.
in a coil, by hydrogen bonding
E.
in a double helix
Question #22
Disulfide bonds exist only in tertiary and quaternary structures.
A.
TRUE
B.
FALSE
Question #23
The primary structure of a protein chain is
A.
determined by the side chains
B.
determined by the types of bonds it contains
C.
the order of amino acids
D.
the overall shape of the protein
E.
the arrangement of the chain in the long molecule
Question #24
An acid can denature a protein by ________.
A.
removing helping molecules such as heme
B.
disrupting hydrophobic interactions within a protein chain
C.
breaking disulfide bridges
D.
disrupting salt bridges between side chains
E.
agitating the protein chains
Question #25
Heavy metals denature proteins by ________.
A.
disrupting salt bridges
B.
changing the temperature of the protein solution
C.
disrupting hydrophobic interactions
D.
releasing amino acids
E.
disrupting disulfide bonds
Question #26
Detergents denature proteins by interfering with the hydrophobic interactions in the proteins structure
A.
TRUE
B.
FALSE
Question #27
Reducing agents disrupt the hydrogen bonds.
A.
FALSE
B.
TRUE
Question #28
Heat increases the kinetic energy and causes the molecules to vibrate so rapidly and violently that the covalent interactions are disrupted.
A.
TRUE
B.
FALSE
Question #29
Since denaturation reactions are not strong enough to break the peptide bonds, the primary structure (sequence of amino acids) remains the same after a denaturation process.
A.
TRUE
B.
FALSE
Question #30
The attractive forces that are important in the secondary structure of a protein are ________.
A.
salt bridges
B.
hydrogen bonds
C.
disulfide bonds
D.
peptide bonds
E.
hydrophobic interactions
Question #31
The analysis of a protein for its amino acid content is valuable in determining the protein's
A.
primary structure
B.
tertiary structure
C.
secondary structure
D.
main structure
E.
quaternary structure
Question #32
A disulfide bond, also called an S-S bond, or disulfide bridge, is a covalent bond derived from two thiol groups.
A.
TRUE
B.
FALSE
Question #33
A protein with a quaternary structure has multiple subunits.
A.
TRUE
B.
FALSE
Question #34
The pitch of a helix contains 3.6 amino acids.
A.
FALSE
B.
TRUE
Question #35
Tertiary structure arises from the interaction of amino acids that are close by in the primary structure.
A.
FALSE
B.
TRUE
Question #36
Fibrous proteins are typically soluble in water.
A.
TRUE
B.
FALSE
Question #37
In an alpha helix, all of the H bonds lie parallel to the helix axis and all of the carbonyl groups are pointing in one direction along the helix axis while the N-H groups are pointing in the opposite direction.
A.
FALSE
B.
TRUE
Question #38
When a protein has two or more polypeptide subunits, their arrangement in space is referred to as quaternary structure.
A.
TRUE
B.
FALSE
Question #39
Which of the following is not a component of tertiary structure?
A.
Disulfide bonds
B.
Hydrogen bonds
C.
Hydrophobic interactions
D.
Ionic bonds
E.
Interactions between two or more sub-units
Question #40
2-mercaptoethanol is a chemical agent used in denaturing proteins. Its primary method of denaturing involves separating disulfide bonds. Based on this method of denaturation, what is the lowest level of protein structure affected by 2-mercaptoethanol?
A.
Primary structure
B.
Quaternary structure
C.
Secondary structure
D.
Tertiary structure
Question #41
The only amino acid that can form disulfide bonds is methionine
A.
TRUE
B.
FALSE
Question #42
A beta-sheet is formed by hydrogen bonding between the hydrogen of an amine group and the backbone carbonyl group.
A.
TRUE
B.
FALSE
Question #43
Within the α helix, the atoms of peptide bonds participates in hydrogen bonding.
A.
TRUE
B.
FALSE
Question #44
The α helix and beta sheet are examples of ___________structures
A.
Primary
B.
Tertiary
C.
Secondary
D.
Quaternary
Need help with your exam preparation?
Get Answers to this exam for $6 USD.
Get Answers to all exams in [ Chem 221 - Biochemistry for Science Majors ] course for $25 USD.
Existing Quiz Clients Login here