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Biochem (Lec)

Total questions: 51

Worksheet time: 1hrs 5mins

Name
Class
Date
1.

the continual degradation and synthesizing of protein

a)

Protein Synthesis

b)

Protein Digestion

c)

Protein turnover

2.

Results from a severe deficiency in kilocalories

a)

Marasmus

b)

Amino Acid Metabolism

c)

Marasmic Kwashiorkor

3.

Consuming too much protein from animal sources increase saturated fat intake

a)

True

b)

False

4.

PEM is not caused by inadequate protein and/or kilocalorie intake

a)

True

b)

False

5.

Severe protein deficiency

a)

Marasmus

b)

Kwashiorkor

6.

distinct in structure compared to other amino acids because its amino group is cyclical

a)

central carbon atom

b)

carboxyl group

c)

Proline

7.

Indole ring side chain, aromatic

a)

Trp

b)

Phe

c)

Met

8.

hydrocarbon aromatic ring

a)

Trp

b)

Phe

c)

Met

9.

Sulfur atom in side chain

a)

Trp

b)

Phe

c)

Met

10.

The side chain imidazole group of histidine is a Heterocyclic aromatic amine

a)

Guanidine Group

b)

Imidazole Group

c)

carboxyl group

11.

In amino acid, carboxyl group (-) and amino group (+) are charged at neutral pH.

a)

True

b)

False

12.

The three-dimensional form of the antiparallel b-pleated sheet arrangement. The chains do fold back on each other but are in a fully extended conformation

a)

True

b)

False

13.

a repetitive supersecondary structure formed when an antiparallel sheet doubles back on itself

a)

ᵦ-meander

b)

ᵦαᵦ unit

c)

Greek key

14.

created when ᵦ-sheets are extensive enough to fold back on themselves

a)

Greek key

b)

ᵦ-barrel

c)

ᵦ-meander

15.

an antiparallel sheet formed by a series of tight reverse turns connecting stretches of a polypeptide chain

a)

ᵦ-meander

b)

Greek key

c)

ᵦαᵦ unit

16.

the polypeptide backbone coils around an imaginary helix axis in clockwise direction

a)

Alpha helix

b)

Secondary structure

17.

Disulfide (-S-S-) bonds between side chains of cysteines

a)

Supersecondary Structures

b)

Covalent interactions

c)

Secondary structure

18.

Hydrogen bonding between polar side chains (e.g., Ser and Thr)

a)

Noncovalent interactions

b)

Tertiary (3°) structure

c)

The Triple Helix of collagen

19.

the association of polypepetide monomers into multisubunit proteins. Some common multi-subunits include:

(a)  

20.

proteins which are folded to a more or less spherical shape

a)

Fibrous Proteins

b)

Globular proteins

21.

Proteins that do not fold correctly may interact with other proteins in an undesired manner and aggregates may result.

a)

True

b)

False

22.

In the protein-dense environment of a cell, proteins may not begin to fold incorrectly or may associate with other proteins before folding is completed

a)

True

b)

False

23.

Hydrophobic interactions are major factors in protein folding

a)

True

b)

False

24.

contain polypeptide chains organized approximately parallel along a single axis

a)

Globular proteins

b)

Fibrous Proteins

25.

the arrangement in space of all atoms in a polypeptide chain

a)

Tertiary (3°) structure

b)

Quaternary 4˚ structure

26.

arrangement of monomer subunits with respect to each other

a)

Tertiary (3°) structure

b)

Quaternary 4˚ structure

27.

the sequence of amino acids in a polypeptide chain, read from the N-terminal end to the C-terminal end

a)

1 st structure

b)

2 structure

28.

the polypeptide backbone is nearly fully extended

a)

Beta sheet secondary structure

b)

Supersecondary structures

c)

2 structure

29.

Isoelectric pH (pl) is the pH at which the majority of molecules of a compound in solution have no net charge

a)

False

b)

True

30.

side chain is a guanidino group

a)

Arg

b)

His

c)

Lys

31.

side chain NH3 group is attached to an aliphatic hydrocarbon chain

a)

Arg

b)

His

c)

Lys

32.

side chain is an imidazole group

a)

Arg

b)

His

c)

Lys

33.

Thyroxine is found only in the thyroid gland

a)

True

b)

False

34.

Hydroxylysine and Hydroxyproline are found only in a few connective tissues such as protein

a)

True

b)

False

35.

For 19 of the 20, the α-amino group is primary; for proline, it is secondary

a)

True

b)

False

36.

a compound that contains both an amino group and a carboxyl group

a)

Amino acid

b)

Protein

c)

Structure Analysis

37.

Deficiency of Protein may lead to: (give three)

(a)  

38.

When the amino acid pool reaches capacity the amino acids are broken down to their component parts for other uses

a)

Amino Acid Absorption

b)

Deamination

c)

Amino Acid Metabolism

39.

Amino acids are transported to the liver from the intestines via the portal vein

a)

Amino Acid Absorption

b)

Amino Acid Metabolism

c)

Deamination

40.

Liver metabolizes amino acids, depending on bodily needs

a)

Amino Acid Absorption

b)

Amino Acid Metabolism

c)

Deamination

41.

Four levels of structure

4 lines
42.

Structure of Proteins

4 lines
43.

Functions of Proteins (give three)

4 lines
44.

the association of polypepetide monomers into multisubunit proteins. Some common multi-subunits include:

4 lines
45.

Example of Fibrous Protein

4 lines
46.

Two steroisomers of amino acids

4 lines
47.

Proteins are abundant in:

4 lines
48.

Adults should consume ______ of protein

4 lines
49.

Premature infants lack sufficient ______ needed to create ______

4 lines
50.

The sequence of amino acids is determined by:

4 lines
51.

Functions of Proteins (give three)

4 lines