Free Printable The levels of structural organization of proteins.

1.

What is the name for the variable region of the 20 amino acids?

a)

Carboxil group

b)

Amino group

c)

R-group

d)

Alpha carbon

2.

What functional group must be present in the R group of an acidic (-) amino acid?

a)

Carboxyl group

b)

Amino group

c)

Hydroxyl group

d)

Carbonyl group

e)

Sulfahydryl group

3.

What functional group must be present in the R group of a basic (+) amino acid?

a)

Carboxyl group

b)

Amino group

c)

Hydroxyl group

d)

Carbonyl group

e)

Sulfahydryl group

4.

What functional group is most often present in a neutral, yet hydrophilic, amino acid’s R group?

a)

Carboxyl group

b)

Amino group

c)

Hydroxyl group

d)

Carbonyl group

e)

Sulfahydryl group

5.

What functional group in cysteines allows them to form strong covalent bonds that stabilize a protein’s tertiary structure?

a)

Carboxyl group

b)

Amino group

c)

Hydroxyl group

d)

Carbonyl group

e)

Sulfahydryl group

6.

How do alpha helices and Beta pleated sheets compare?

a)

They are both forms of protein secondary structure

b)

They are both formed due to formation of H bonds between N-H and C=O groups along the backbon of polipeptide chain

c)

The beta sheets are more rigid and strong because they form more abundant H bonds

d)

All of the avobe

7.

Haemoglobin is a globular protein with quaternary structure.

Fig 1.1 is a diagram of the haemoglobin molecule.

Determine the name of the labelled X ?

a)

haem

b)

amino group

c)

carboxyl group

d)

radical

8.

Which arrow points to a peptide bond?

a)

a

b)

b

c)

c

d)

d

9.

Which amino acids tend to cluster in the center of an aqueous protein, but to be located on the outer edges of proteins located within a cell membrane’s lipid bilayer?

a)

Acidic amino acids

b)

Basic amino acids

c)

Disulfide bridge forming cycteines and methionones

d)

Polar, hydrophilic amino acids

e)

Nonpolar, hydrophobic amino acids

10.

R group interactions control which levels of protein folding?

a)

Ptimary structure and secondary structure

b)

secondary structure only

c)

Tetiary structure and quaternary structure

d)

Tetiary structure only

e)

quaternary structure only

11.

Fig 2.1 shows the prymary structure of a lysozyme molecule, an enzyme found in tears, saliva and in lysosomes.

What is meant by the term

'primary structure'

a)

conformational arrangement of the main chain of the macromolecule

b)

sequence of amino acids in a polypeptide chain

c)

overall three-dimensional arrangement of its polypeptide chain in space

d)

the association of several protein chains into a closely packed arrangement

12.

The name of the structures responsible for holding the two polipeptide chains together.

a)

hydrogen bonds

b)

disulfide bonds

c)

inonisc bonds

d)

gydrophilic bonds

13.

Determine the shape and structural level of hemoglobin protein.

a)

Alpha-helix,

secondary structure

b)

fibrous,

primary structure

c)

globular,

quaternary structure

d)

beta pleated sheet,

tertiary structure

14.

The amino acid sequence of the protein hormone insulin is shown Fig 3.1.

Which two levels of protein structure are shown?

a)

primary

quaternary

b)

only primary

c)

alpha-helix

beta-pleated sheet

d)

primary

secondary

15.

Penicillin is an antibiotic that interferes with the synthesis of cell walls in bacteria. Even before became widely available in the 1940s, the enzyme penicillinase which breaks down pinicillin had been isolated. THis enzyme is now found in many bacteria and gives them resistance to penicillin.

Fig 7.1 is a ribbon model of the structure of the enzyme penicillinase. The arrow indicates the active site of the enzyme.

IIdentify the aspects of protein structure shown.

a)

amino acids,

bena pleated sheet

b)

R-groups,

hydrogen bonds

c)

prosthetic groups,

disulfide bonds

d)

alpha helix,

bena pleated sheet

16.

Penicillin is an antibiotic that interferes with the synthesis of cell walls in bacteria. Even before became widely available in the 1940s, the enzyme penicillinase which breaks down pinicillin had been isolated. THis enzyme is now found in many bacteria and gives them resistance to penicillin.

Fig 7.1 is a ribbon model of the structure of the enzyme penicillinase. The arrow indicates the active site of the enzyme.

IIdentify the aspects of protein structure not shown.

a)

primary structure,

secondary structure

b)

alpha helix,

beta pleated sheet

c)

peptide,

hydrogen bonds

d)

globular,

tertiary structure

17.

Cholera is a disease caused by the bacterium vibrio cholerae. The disease symptoms are caused by toxin, produced by the bacterium, interacting with in the cell surface membranes of epithelial cells in the human intestine.

The cholera toxin is a protein and is composed of two subunits, A and B. Subunit A is made from one polipeptide and subunit B is made five identical polipeptides.

Fig.9.1 shows the structure of the cholera toxin.

Name the level of structure that is only shown by a protein that has more than one polipeptide chain?

a)

primary structure

b)

secondary structure

c)

tertiary structure

d)

quaternary structure

18.

Cholera is a disease caused by the bacterium vibrio cholerae. The disease symptoms are caused by toxin, produced by the bacterium, interacting with in the cell surface membranes of epithelial cells in the human intestine.

The cholera toxin is a protein and is composed of two subunits, A and B. Subunit A is made from one polipeptide and subunit B is made five identical polipeptides.

Fig.9.1 shows the structure of the cholera toxin.

Name the part labelled S ?

a)

sequence amino acids

b)

alpha helix

c)

polipeptides

d)

beta pleated sheet

19.

Haemoglobin is a globular protein with quaternary structure.

Fig 1.1 is a diagram of the haemoglobin molecule.

Determine the function of the labelled X ?

a)

store of energy

b)

forms a peptide bonds

c)

carries oxygen

d)

gives a globular shape

20.

How a globular protein differs from fibrous protein, such as collagen?

a)

insolible, hydrophobic groups

b)

solible, hydrophilic groups

c)

contains many amino acids

d)

performs a specific function

The levels of structural organization of proteins.

Total questions: 20

Worksheet time: 11mins

Similar Resources on Wayground