ACTIVITY 2M Protein and its structuree

Question 1

This type of proteins provides protection and support that have very specialized properties.

Answer 1

structural proteins

Question 2

The heme in hemoglobin is a(n)

Answer 2

small molecule within a protein

Question 3

Given are three (3) Statements:

(1) Some tertiary-structure interactions involve covalent bonding.
(2) Nonpolar amino acids contain one amino group, one carboxyl group, and a nonpolar side chain.
(3) The two amino acids present in a dipeptide are linked via an amide linkage.

Answer 3

All three correct

Question 4

What do you call a genetic disease wherein red cells assumes a sickle cell shape?

Answer 4

sickle cell anemia

Question 5

These are proteins that result from the decomposition of simple and compound proteins.

Answer 5

derived protein

Question 6

Fibrous protein is made predominantly of what type of secondary structure?

Answer 6

beta pleated sheet

Question 7

The complete hydrolysis of a protein produces a mixture of

Answer 7

free amino acids

Question 8

Denaturation of a protein

Answer 8

disrupts the secondary, tertiary or quaternary structure of a protein

Question 9

What is the main reason the peptide bond cannot be rotated?

Answer 9

Because it has double bond on the O attached to alpha
carbon

Question 10

Which of the following terms describes a protein secondary structure?

Answer 10

alpha helix

Question 11

Determine the structural level (primary, secondary, tertiary, quaternary) associated with each of the protein
characteristics.

Characteristic:
Sequence of amino acids in a protein chain

Answer 11

primary structure

Question 12

In a sickle-cell anemia, the hemoglobin molecules

Answer 12

clump together into insoluble fibers

Question 13

This structure of protein refers to the unique 3-D conformations that globular proteins assume as they fold onto their native (biologically active) structure.

Answer 13

tertiary structure

Question 14

Hemoglobin is an example of a protein with

Answer 14

globular structure

Question 15

What type of non-covalent bond stabilizes the alpha helix and the beta pleated sheet structure of proteins?

Answer 15

hydrogen bond

Question 16

Which of the following is an incorrect characterization for the protein hemoglobin?

Answer 16

simple protein

Question 17

Heavy metals (toxic metals) denature proteins by

Answer 17

disrupting disulfide bonds

Question 18

Which of the following statements concerning the tripeptide Val-Ala-Gly is correct?

Answer 18

Three peptide linkages are present.

Question 19

This is a good example of a beta pleated sheet.

Answer 19

silk

Question 20

To which of the following levels of protein structure is the sequence of amino acids in a protein directly related?

Answer 20

primary

Question 21

These are types of protein that connect the human system into the surroundings.

Answer 21

sensory

Question 22

How many different tripeptides can be formed from two molecules of leucine (Leu) and one molecule of glutamic acid (Glu)?

Answer 22

five

Question 23

It is considered an important fibrous protein that binds cell together to make tissues secreted from cells and
assemble in long fibers.

Answer 23

Extracellular matrix

Question 24

How many peptide linkages are present in a tripeptide?

Answer 24

three

Question 25

In the tetrapeptide Phe-Gln-Trp-His, the C-terminal amino acid is

Answer 25

His

Question 26

This protein structure is considered the overall shape of the protein.

Answer 26

tertiary structure

Question 27

What are the two types of secondary structure found in proteins?

Answer 27

alpha helix and beta pleated sheets

Question 28

Below are constraints in the formation of helical structures in protein EXCEPT glycine valine proline

Answer 28

proline

Question 29

Hemoglobin has a total of _________ protein chains in its quaternary structure.

Answer 29

four

Question 30

This is an important fibrous protein wherein glycine is present every third amino acid in the chain.

Answer 30

collagen

Question 31

Interactions between amino acid R groups that gives the final shape (or conformation) of protein is responsible for which of the following levels of protein structure?

Answer 31

tertiary

Question 32

Quaternary structure is possible for a protein only when:

Answer 32

Two or more protein chains are present.

Question 33

The function of myoglobin is to

Answer 33

carry oxygen in the muscles

Question 34

Which among the choices below is an example of storage protein?

Answer 34

ferritin

Question 35

Below are examples of defense proteins EXCEPT thrombin keratin hemoglobin fibrinogen immunoglobulins

Answer 35

Hemoglobin/thrombin

Question 36

Sensory protein

Answer 36

Tsp-O

Question 37

Defense protein

Answer 37

fibrinogen

Question 38

Storage protein

Answer 38

ferritin

Question 39

Regulatory protein

Answer 39

insulin

Question 40

Stress response protein

Answer 40

cytochrome P - 450

Question 41

Transport protein

Answer 41

hemoglobin

Question 42

Enzymic protein

Answer 42

Phenylalanine - N - methyl

Question 43

Structural protein

Answer 43

elastin

Question 44

Which of the following types of interactions contribute to protein tertiary structure?

Answer 44

Hydrogen bonds between C=O and N-H groups

Question 45

This level of structure in protein occur when there is a strong hydrogen bonding between a carbonyl group and the amide group of the nearest amino acid with which it

Answer 45

Helical structure

Question 46

Given are three (3) Statements: - (1) In a peptide, the number of amino acids and the number of peptide bonds are always equal - (2) HDL and LDL are examples of lipoproteins. - (3) Tertiary structure interactions in proteins always involve amino acid R groups.

Answer 46

Only one