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 Secondary

B Tertiary

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 TRUE

B FALSE

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 Primary structure

B Tertiary structure

C Secondary structure

D Quaternary structure

Question #6

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

A Hydrophobic interactions

B Disulfide bonds

C Ionic bonds

D Interactions between two or more sub-units

E Hydrogen bonds

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 FALSE

B TRUE

Question #9

Fibrous proteins are typically soluble in water.

A FALSE

B TRUE

Question #10

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

A FALSE

B TRUE

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 FALSE

B TRUE

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 secondary structure

B quaternary structure

C primary structure

D tertiary structure

E main structure

Question #15

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

A disulfide bonds

B salt bridges

C hydrophobic interactions

D hydrogen bonds

E peptide bonds

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 TRUE

B FALSE

Question #18

Reducing agents disrupt the hydrogen bonds.

A FALSE

B TRUE

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 releasing amino acids

B disrupting salt bridges

C disrupting hydrophobic interactions

D disrupting disulfide bonds

E changing the temperature of the protein solution

Question #21

An acid can denature a protein by ________.

A disrupting hydrophobic interactions within a protein chain

B breaking disulfide bridges

C disrupting salt bridges between side chains

D agitating the protein chains

E removing helping molecules such as heme

Question #22

The primary structure of a protein chain is

A determined by the side chains

B the overall shape of the protein

C the order of amino acids

D the arrangement of the chain in the long molecule

E determined by the types of bonds it contains

Question #23

Disulfide bonds exist only in tertiary and quaternary structures.

A FALSE

B TRUE

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 double helix

B in a coil, by hydrogen bonding

C by hydrogen bonding between different sections of the polypeptide chain

D in random order, due to hydrophobic interactions

E in a triple helix

Question #25

Disulfide bonds in a protein chain connect ________.

A two asparagine residues

B an amine and a carboxylic acid group

C an alcohol 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 changes in primary structure

B the binding of toxic compounds

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 alpha helix

B primary structure

C tertiary structure

D beta sheet

Question #28

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

A Primary structure

B Secondary structure

C Net charge

D Tertiary structure

Question #29

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

A peptide bonds

B Van der Waals interactions

C hydrogen bonds

D disulfide bridges

E salt bridges

Question #30

What does the quaternary structure of a protein involve?

A partial denaturation

B random coil alternating with a-helix

C the complete three-dimensional conformation

D the association of two or more peptide chains

Question #31

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

A Hydrogen bonding between R groups

B Disulfide bonds between cysteine residues

C Hydrogen bonding between an amine and carbonyl group

D Peptide bonding between amino acids

E Hydrophobic interactions

Question #32

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

A TRUE

B FALSE

Question #33

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

A Globular

B Fibrous

C Integral

D Peripheral

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 FALSE

B TRUE

Question #37

Because of the geometry of the individual amino acids, the hydrogen bonds of an antiparallel beta sheet occur at an angle.

A TRUE

B FALSE

Question #38

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

A FALSE

B TRUE

Question #39

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

A FALSE

B TRUE

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 TRUE

B FALSE

Question #41

The pitch of a helix is 3.6 angstroms.

A FALSE

B TRUE

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 FALSE

B TRUE

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 TRUE

B FALSE

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L6 3D Structure of Proteins Part 2 of 2

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