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Lecture 2 Quiz

Total questions: 20

Worksheet time: 20mins

Name
Class
Date
1.

What is the correct order of protein structures from simplest to most complex?

a)
Primary structure, Secondary structure, Tertiary structure, Quaternary structure
b)
Quaternary structure, Tertiary structure, Secondary structure, Primary structure
c)
Primary structure, Tertiary structure, Secondary structure, Quaternary structure
d)
Secondary structure, Primary structure, Tertiary structure, Quaternary structure
2.

What is the main difference between Type I and Type II turns in protein structures?

a)

Dihedral angles of central residues

b)

Number of amino acids involved

c)

Presence of hydrogen bonds

d)

Involvement of glycine residues

3.

What is the distinguishing feature of an amphipathic α helix?

a)

Extended conformation

b)

Distinct hydrophobic and hydrophilic faces

c)

Presence of proline residues

d)

Tight coiling around an axis

4.

What is the purpose of loop regions in protein structures?

a)

Stabilize the protein core

b)

Provide flexibility to the structure

c)

Form hydrogen bonds with polar groups

d)

Connect alpha helices and beta strands

5.

What is the function of the calcium-binding EF-hand motif?

a)

Enhance enzymatic activity

b)

Facilitate protein folding

c)

Bind calcium ions

d)

Promote protein-protein interactions

6.

What is the structural arrangement of the Greek key motif?

a)

Helix-turn-helix motif for DNA binding

b)

Coiled-coil structure with repeating distance

c)

Parallel β strands connected by an α helix

d)

Antiparallel β sheet with specific strand arrangement

7.

What is the characteristic of coiled-coil structures?

a)

Form superhelix with repeating distance

b)

Involve long dimeric coiled coils

c)

Found in proteins that make up muscle fiber

d)

Facilitate protein dimerization

8.

What is the purpose of β-α-β motifs in protein structures?

a)

Connect parallel β strands with an α helix

b)

Promote ligand binding

c)

Facilitate protein-protein interactions

d)

Enhance structural stability

9.

What is the structure of the DNA binding domains of the transcription factors Fos and Jun?

a)

A repeating helical structure known as the armadillo motif

b)

A closed β barrel

c)

A four-helix bundle protein

d)

Two α helices that coil around each other

10.

What is the pattern of amino acids in a parallel coiled coil?

a)

c, b, a, g, f, e, d

b)

g, f, e, d, c, b, a

c)

a, b, c, d, e, f, g

d)

d, e, f, g, a, b, c

11.

What can stabilize coiled-coil structures?

a)

Van der Waals contacts

b)

Hydrogen bonds

c)

Disulfide bonds

d)

Ionic interactions

12.

What is the structure of bacteriorhodopsin?

a)

Seven transmembrane helices

b)

A porin with 16 β strands forming a barrel

c)

A closed β barrel

d)

A repeating helical structure known as the armadillo motif

13.

What is the function of porins?

a)

Bind to DNA

b)

Form transmembrane channels

c)

Act as enzymes

d)

Transport metabolites

14.

What is the role of charged residues in bacteriorhodopsin?

a)

Stabilize the protein structure

b)

Act as cofactors

c)

Line a proton conducting conduit

d)

Form hydrogen bonds with lipids

15.

How are transmembrane α helices stabilized in membrane proteins?

a)

Van der Waals contacts and hydrogen bonds

b)

Disulfide bonds

c)

Ionic interactions

d)

Hydrophobic interactions

16.

How many residues are approximately required for an α helix to span a lipid bilayer?

a)

25-30

b)
40-45
c)

60-65

d)
10-15
17.

What method is commonly used to predict transmembrane α-helices from amino acid sequences?

a)
Hydrophobicity analysis
b)
Nucleotide sequencing
c)
Protein folding
d)
Amino acid synthesis
18.

In the context of protein structure, what does the term "amphipathic" specifically refer to?

a)
Term used for proteins with no distinct regions
b)
Molecule or structure with both hydrophilic and hydrophobic regions
c)
Structure with only hydrophobic regions
d)
Molecule with only hydrophilic regions
19.

What feature of α-helices allows them to satisfy hydrogen bonding requirements within the lipid bilayer?

a)

Their amphipathic nature

b)
Lack of hydrogen bonding
c)
Inability to form hydrogen bonds
d)

The internal hydrogen bonding between backbone NH and C=O groups

20.

How are binding sites in proteins typically located in relation to their structure?

a)
Specific regions on the protein surface such as cavities, clefts, or pockets.
b)
Located on the exterior of the cell membrane
c)
Only in the core of the protein
d)
Randomly scattered throughout the protein structure