Biochemistry Proteins

Front 1

What are the functions of proteins?

Back 1

1- Catalytic Functions.
2- Transport Functions.
3- Contractile Functions.
4- Protective Functions.
5- Regulatory Functions.

Front 2

Histones' special functions are

Back 2

They are closely associated with DNA, they control & regulate gene transcription & translation.

Front 3

Define axial ration

Back 3

Length / Width

Front 4

Fibrous proteins are water .....

Back 4

insoluble

Front 5

The axial ration of fibrous proteins is:

Back 5

>=10

Front 6

The axial ration of globular proteins is:

Back 6

<=4

Front 7

How are the proteins chemically classified?:

Back 7

1- Simple proteins.
2- Conjugated proteins.
3- Derived proteins.

Front 8

Protamis are ..... proteins

Back 8

simple proteins

Front 9

Prolamins are ...... proteins

Back 9

simple proteins

Front 10

Name 2 prolamin proteins

Back 10

Zein of corn
Gliadin of wheat

Front 11

...... are simple structural proteins

Back 11

Scleroproteins

Front 12

Name 2 simple proteins which are soluble in water:

Back 12

1- Albumin.
2- Protamins.

Front 13

Name 2 simple proteins which denature with heat:

Back 13

1- Albumin.
2- Globulins.

Front 14

Name 2 simple proteins which preciptate in amm sulfate solutions:

Back 14

1- Albumins. (fully saturated)
2- Globulins. (Half saturated)

Front 15

Globulins aren't soluble in water but they're soluble in:

Back 15

dilute salt solution.

Front 16

Protamins are rich in

Back 16

Arginine & Lysine Residues

Front 17

Prolamins are soluble in

Back 17

70-80% alcohol solution

Front 18

Scleroproteins are soluble in

Back 18

hot strong acids

Front 19

the non-protein part in a conjugated protein is called

Back 19

prothetic group

Front 20

Proteins are classified on the basis of the chemical nature of their prothetic group into:

Back 20

1- Glycoproteins.
2- Lipoproteins.
3- Nucleoproteins.
4- Phosphoproteins.
5- Chromoproteins.
6- Metalloproteins.

Front 21

All proteins of the pituitary are

Back 21

glycoproteins except for oxytocin & vasopressin

Front 22

What is the protein when the carbohydrate content is more than 10% of the whole protein molecule

Back 22

mucoproteins or proteoglycans

Front 23

Chylomicrons are

Back 23

lipoproteins

Front 24

Casein of milk is a

Back 24

phosphoprotein

Front 25

VLDL, LDL, HDL are

Back 25

Lipoproteins

Front 26

A protein with a yellow-colored prothetic group is

Back 26

Riboflavin

Front 27

A protein with a red-colored prothetic group

Back 27

Hemoglobin

Front 28

A protein with a purple-colored prothetic group

Back 28

Visual purple(Vit.A)
(Rhodopsin)

Front 29

A protein with a green-colored prothetic group

Back 29

Chlorophyll

Front 30

Copper-containing metalloprotein found in plasma

Back 30

Ceruloplasmin

Front 31

Copper containing enzyme essential for collagen synthesis

Back 31

Lysl Oxidase Enzyme

Front 32

Carbonic anhydrase contains

Back 32

Zinc

Front 33

Iron containing proteins are subdivided into:

Back 33

1- Heme-containing proteins.
2- Non Heme-containing proteins.

Front 34

List some example of heme-containing proteins

Back 34

Hemoglobin
Myoglobin
Cytochrome Oxidase
Cytochrome p-450
Catalase
Tryptophan pyrrolases.

Front 35

List some examples of non heme-containing proteins

Back 35

Ferritin
Transferrin
Lactoferrin

Front 36

The only bonds that can't be broken by denaturation agents

Back 36

Peptide bonds

Front 37

Name 2 agents which break the sulfide bond

Back 37

beta-mercaptoethanol
performic acid

Front 38

Van der waal's forces occur at a distance of

Back 38

3-4 A(contact distance)

Front 39

protein coformation

Back 39

the proteins after interactive forces has taken place between the AAs of the protein

Front 40

Native proteins

Back 40

Proteins in their functional, folded conformation.

Front 41

List the main bonds which distinguish each of the following protein structures:
1- Primary.
2- Secondary.
3- Tertiary

Back 41

1- Peptide bonds.
2- Hydrogen bonds.
3- All of the other forces, esp. disulfide bonds.

Front 42

The types of secondary structures are

Back 42

1- Alpha Helices.
2- Beta pleated sheets.
3- Beta turns.

Front 43

The alpha helices' structure is stabilized by

Back 43

Intrachain hydrogen bonds

Front 44

Each turn of the alpha helix consists of .... AA

Back 44

3.6

Front 45

The alpha helix occurring in most proteins is .... handed

Back 45

right

Front 46

Disruptions of the alpha helix may occur due to:

Back 46

1- Steric effect by bulky amino acids.
2- Proline's N which is a part of a hard ring structure.
3- Electrostatic repulsions.

Front 47

The two types of beta pleated sheets are

Back 47

parallel
antiparallel

Front 48

The beta pleated structure is rigid, therefore it can be found in

Back 48

fibrous proteins

Front 49

A polypeptide unit in the quaternary structure of a protein is called

Back 49

monomer
protomer

Front 50

Amyloid

Back 50

protein deposits

Front 51

Physical factors which lead to denaturation are:

Back 51

1- High temperature
2- Vigorous Shaking.
3- High Pressure.
4- U.V & X-Ray radiations.

Front 52

Chemical factors leading to denaturation are

Back 52

1- Strong acids and bases(irreversible)
2- Beta-mercaptoethanol.
3- Sodium dodecyl sulfate(SDS)
4- Concentrated urea.

Front 53

.... is used in laboratories to denature plasma proteins

Back 53

Trichloroacetic acid