L6 3D Structure of Proteins Part 2 of 2

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Question #1

The α helix and beta sheet are examples of ___________structures

A Tertiary

B Secondary

C Primary

D Quaternary

Question #2

Within the α helix, the atoms of peptide bonds participates in hydrogen bonding.

A FALSE

B TRUE

Question #3

A beta-sheet is formed by hydrogen bonding between the hydrogen of an amine group and the backbone carbonyl group.

A FALSE

B TRUE

Question #4

The only amino acid that can form disulfide bonds is methionine

A TRUE

B FALSE

Question #5

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 Quaternary structure

B Tertiary structure

C Primary structure

D Secondary structure

Question #6

Which of the following is not a component of tertiary structure?

A Interactions between two or more sub-units

B Ionic bonds

C Disulfide bonds

D Hydrogen bonds

E Hydrophobic interactions

Question #7

When a protein has two or more polypeptide subunits, their arrangement in space is referred to as quaternary structure.

A FALSE

B TRUE

Question #8

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 TRUE

B FALSE

Question #9

Fibrous proteins are typically soluble in water.

A TRUE

B FALSE

Question #10

Tertiary structure arises from the interaction of amino acids that are close by in the primary structure.

A TRUE

B FALSE

Question #11

The pitch of a helix contains 3.6 amino acids.

A TRUE

B FALSE

Question #12

A protein with a quaternary structure has multiple subunits.

A TRUE

B FALSE

Question #13

A disulfide bond, also called an S-S bond, or disulfide bridge, is a covalent bond derived from two thiol groups.

A FALSE

B TRUE

Question #14

The analysis of a protein for its amino acid content is valuable in determining the protein’s

A tertiary structure

B primary structure

C main structure

D quaternary structure

E secondary structure

Question #15

The attractive forces that are important in the secondary structure of a protein are ________.

A disulfide bonds

B hydrophobic interactions

C hydrogen bonds

D peptide bonds

E salt bridges

Question #16

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 #17

Heat increases the kinetic energy and causes the molecules to vibrate so rapidly and violently that the covalent interactions are disrupted.

A FALSE

B TRUE

Question #18

Reducing agents disrupt the hydrogen bonds.

A TRUE

B FALSE

Question #19

Detergents denature proteins by interfering with the hydrophobic interactions in the proteins structure

A FALSE

B TRUE

Question #20

Heavy metals denature proteins by ________.

A disrupting salt bridges

B releasing amino acids

C changing the temperature of the protein solution

D disrupting hydrophobic interactions

E disrupting disulfide bonds

Question #21

An acid can denature a protein by ________.

A disrupting hydrophobic interactions within a protein chain

B agitating the protein chains

C removing helping molecules such as heme

D breaking disulfide bridges

E disrupting salt bridges between side chains

Question #22

The primary structure of a protein chain is

A the overall shape of the protein

B the arrangement of the chain in the long molecule

C determined by the side chains

D the order of amino acids

E determined by the types of bonds it contains

Question #23

Disulfide bonds exist only in tertiary and quaternary structures.

A TRUE

B FALSE

Question #24

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 in a triple helix

B in a double helix

C in random order, due to hydrophobic interactions

D by hydrogen bonding between different sections of the polypeptide chain

E in a coil, by hydrogen bonding

Question #25

Disulfide bonds in a protein chain connect ________.

A an alcohol and a carboxylic acid group

B two asparagine residues

C an amine and a carboxylic acid group

D tryptophan and alanine residues

E two cysteine residues

Question #26

The term “denaturation,” when used in conjunction with proteins or nucleic acids, refers to a change in structural characteristics primarily due to __________.

A the binding of toxic compounds

B changes in primary structure

C the disruption of non-covalent bonds

D the disruption of covalent bonds

Question #27

A structure that has hydrogen bonds between polypeptide chains arranged side by side is

A primary structure

B beta sheet

C tertiary structure

D alpha helix

Question #28

Which of the following properties of a protein is least likely to be affected by changes in pH?

A Primary structure

B Net charge

C Tertiary structure

D Secondary structure

Question #29

What kinds of interactions do NOT contribute to the tertiary protein structure?

A disulfide bridges

B salt bridges

C hydrogen bonds

D peptide bonds

E Van der Waals interactions

Question #30

What does the quaternary structure of a protein involve?

A partial denaturation

B the complete three-dimensional conformation

C the association of two or more peptide chains

D random coil alternating with a-helix

Question #31

Which of the following is an example of the secondary structure of a protein?

A Peptide bonding between amino acids

B Hydrogen bonding between an amine and carbonyl group

C Hydrophobic interactions

D Disulfide bonds between cysteine residues

E Hydrogen bonding between R groups

Question #32

β turns connect the ends of two adjacent segments of a parallel β sheet.

A FALSE

B TRUE

Question #33

Collagen, the most abundant protein in the body, is an example of what type of protein?

A Peripheral

B Fibrous

C Integral

D Globular

Question #34

The side chains of a beta sheet are oriented parallel to the plane of the sheet.

A FALSE

B TRUE

Question #35

Antiparallel beta sheets are more stable than parallel beta sheets.

A FALSE

B TRUE

Question #36

Ala and Leu are strong a-helix formers.

A TRUE

B FALSE

Question #37

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 #38

The stability of an alpha-helix is affected by the side and the identity of the side chains.

A TRUE

B FALSE

Question #39

Each hydrogen bond in a alpha helix closes a loop containing 3.6 atoms.

A TRUE

B FALSE

Question #40

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 #41

The pitch of a helix is 3.6 angstroms.

A TRUE

B FALSE

Question #42

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 TRUE

B FALSE

Question #43

Glycine is often found in the middle of an alpha-helix.

A TRUE

B FALSE

Question #44

Ala and Leu are strong alpha-helix breakers.

A FALSE

B TRUE

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L6 3D Structure of Proteins Part 2 of 2

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