Part 1 Flashcards

1
Q

What are proteins?

A

Proteins are large molecules containing Carbon, Hydrogen, Oxygen, and Nitrogen. Some proteins also contain sulphur.

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2
Q

What percentage of a lean adult body is protein?

A

A lean adult body normally contains 12-18% protein.

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3
Q

How is protein stored in the body?

A

Only small amounts of protein are temporarily stored in the body, which can be quickly used up on demand compared to carbohydrates and lipids.

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4
Q

What do the symbols H, N, C, O, and R represent in proteins?

A

H = Hydrogen, N = Nitrogen, C = Carbon, O = Oxygen, R = Variable Side Chain.

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5
Q

• is a covalent bond that connects each amino acid to another amino acid that is formed through dehydration reaction. The long chains of amino acids are called polypeptides.

A

PEPTIDE BOND (Amide Linkages)

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6
Q

• A protein is a natural polymer composed of amino acid monomers joined together

A

PEPTIDE BOND (Amide Linkages)

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7
Q

The long chains of amino acids

A

polypeptides

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8
Q

• An index used to determine whether physiological requirements are being met.

A

NITROGEN BALANCE

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9
Q

Nitrogen ingested
(Primarily as protein)
-
Nitrogen Excreted
(Primarily as urea)

A

Nitrogen balance

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10
Q

0 (Nitrogen equilibrium)

A

Nitrogen balance

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11
Q

protein degradation

A

Protein synthesis

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12
Q

protein synthesis > protein degradation

A

Positive Nitrogen Balance

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13
Q

protein synthesis < protein degradation

A

Negative Nitrogen Balance

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14
Q

• Most proteins do not occur as long chains inside the cells unlike polysaccharides. Instead, they are folded into three - dimensional structures, which determine the structures and kinds of amino acids.

A

PROTEIN FOLDING

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15
Q

Types of Protein Structures

A

Primary Structure
Secondary Structure Tertiary Structure
Quaternary Structure

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16
Q

• The unique sequencing of amino acids in a polypeptide chain.

A
  1. Primary (1°) Structure
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17
Q

• Localised folding in some regions of the chain of amino acids - alpha helix and beta sheet

A
  1. Secondary (2°) Structure
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18
Q

• Overall shape of a polypeptide as a result of interactions of the R Group and water

A
  1. Tertiary (3°) Structure
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19
Q

• Arrangement of two or more polypeptide chains relative to one another.

A
  1. Quaternary (4º) Structure
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20
Q

2 PROTEIN CLASSIFICATION BASED ON THEIR
CHEMICAL COMPOSITION

A
  1. SIMPLE PROTEINS
  2. COMPLEX PROTEINS
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21
Q

• Only made up of amino acids

A

SIMPLE PROTEINS

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22
Q

• These proteins have other chemical components in addition to amino acids
- organic or inorganic additional components known as “prosthetic groups”

A

COMPLEX PROTEINS

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23
Q

PROSTHETIC
GROUP
-Heme Unit

SPECIFIC EXAMPLE
-Haemoglobin/Hemoglobin
Myoglobin

FUNCTION
-Carries oxygen in the blood Binds oxygen in muscles

A

Haemoproteins/
Hemoproteins

24
Q

PROSTHETIC
GROUP
-Lipid

SPECIFIC EXAMPLE
-Low-density Lipoprotein (LDL)
High-density Lipoprotein (HDL)

FUNCTION
-Carries Lipid

A

Lipoproteins

25
Q

PROSTHETIC
GROUP
-Carbohydrates

SPECIFIC EXAMPLE
-Gamma Globulin
Mucin
Interferon

FUNCTION
-Antibody
Lubricant in mucous secretions
Antiviral protection

A

Glycoproteins

26
Q

PROSTHETIC
GROUP
-Phosphate Group

SPECIFIC EXAMPLE
-Glycogen Phosphorylase

FUNCTION
-Enzyme in glycogen phosphorylation

A

Phosphoproteins

27
Q

PROSTHETIC
GROUP
-Nucleic Acid

SPECIFIC EXAMPLE
-Ribosomes
-Viruses

FUNCTION
-Site for protein synthesis in cells
Self-replicating, infectious complex

A

Nucleoproteins

28
Q

PROSTHETIC
GROUP
-Metal Ion

SPECIFIC EXAMPLE
-Iron - ferritin
-Zinc - alcohol dehydrogenase

FUNCTION
-Storage complex for iron
-Enzyme in alcohol oxidation

A

Metalloproteins

29
Q

PROTEIN CLASSIFICATION BASED ON SHAPE

A
  1. FIBROUS PROTEINS
  2. GLOBULAR PROTEINS
30
Q

• These proteins are spiral and helical and are cross linked by disulphide and hydrogen bonds

A

FIBROUS PROTEINS

31
Q

HIGH PROTEIN VEGETABLES
(RANKED FROM HIGHEST TO LOWEST)

A

GREEN PEAS
SPINACH
ARTICHOKES
CORN
AVOCADO
ASPARAGUS
BRUSSELS
SPROUTS
MUSHROOMS
KALE
POTATOES

32
Q

• They represent about 25-30% of all proteins among vertebrates.

33
Q

• They are found in different tissues and organs, including tendons and the organic matrix of bone - in which they are present in very high percentages.

34
Q

COLLAGEN RICH FOODS
(FOR SKIN)

A

Berries
Leafy Greens
Citrus Fruits
Nuts and Seeds
Soy Products
Tomatoes
Avocado

35
Q

COLLAGEN RICH FOODS
(FOR SKIN)

A

Berries
Leafy Greens
Citrus Fruits
Nuts and Seeds
Soy Products
Tomatoes
Avocado

36
Q

• They constitute almost the entire dry weight of nails, claws, beak, hooves, horns, hair, wool, and a large part of the outer layer of the skin.

A

a -Keratins

37
Q

• This protein provides elasticity to the skin and blood vessels due to its random coiled structure, different from the structures of collagen and
a - keratin.

38
Q

• Most of the proteins belong to this class, in which they have a compact and spherical structure and more complex than fibrous proteins.

A

GLOBULAR PROTEINS

39
Q

They are generally soluble in water but can also be found inserted into biological membranes (transmembrane proteins). Hence, in a hydrophobic environment.

A

GLOBULAR PROTEINS

40
Q

PROTEIN CLASSIFICATION BASED ON FUNCTION

A

Types:
Enzymes
Transport
Structural
Hormones
Defence
Contractile
Storage

41
Q

EXAMPLES
-Digestive enzymes:
Amylase, lipase, pepsin, trypsin

FUNCTIONS
-Serve as catalysts in biochemical reactions such as digestive enzymes, which aid in digestion of food by breaking down nutrients to monomers.

42
Q

EXAMPLES
-Haemoglobin, Albumin

FUNCTIONS
-Carry substances in the blood or lymph throughout the body.

43
Q

EXAMPLES
-Actin, Tubulin, Keratin

FUNCTIONS
-Construct different structures like the cytoskeleton, hair, and nails.

A

Structural

44
Q

EXAMPLES
-Insulin, thyroxine

FUNCTIONS
-Coordinate the activity of different body systems

45
Q

EXAMPLES -Immunoglobulins (Antibodies)

FUNCTIONS
-Protect the body from invading pathogens

46
Q

EXAMPLES
-Actin, myosin

FUNCTIONS
-Effect of muscle contraction - for movement

A

Contractile

47
Q

EXAMPLES
-Legume storage of proteins, egg white (albumin)

FUNCTIONS
-Provide nourishment in early development of the embryo and the seedling.

48
Q

IMMUNOGLOBULINS

A

IgA
IgD
IgE
IgG
IgM

49
Q

Found in mucous, saliva, tears, and breastmilk
Protects us against pathogens
Transferred to an infant through breastmilk and colostrum.

50
Q

Part of the B cell receptor - helps them to start the immune response.
Activates basophils and mast cells

51
Q

Protects against parasitic worms.
Responsible for allergic reactions.
Found mainly on tonsils, skin and mucous membranes.

52
Q

Secreted by plasma cells in the blood
Able to cross the placenta into the fetus - important in the immunity of newborn

53
Q

May be attached to the surface of a B cell or secreted into the blood - with strong agglutinating ability
Responsible for early stages of immunity.

54
Q

• A protein is defined by its 1°, 2°, and 30 structures. These give proteins certain identifying properties - biological, enzymatic, solubility, ionic, reactivity of side group, molecular weight, size, native structure.

A

Denaturation of Proteins

55
Q

-is the result of any changes in the native structure of proteins, which is caused about by breaking of any bond except the peptide bond.

A

Denaturation of Proteins