Part 1 Flashcards

(55 cards)

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

25
PROSTHETIC GROUP -Carbohydrates SPECIFIC EXAMPLE -Gamma Globulin Mucin Interferon FUNCTION -Antibody Lubricant in mucous secretions Antiviral protection
Glycoproteins
26
PROSTHETIC GROUP -Phosphate Group SPECIFIC EXAMPLE -Glycogen Phosphorylase FUNCTION -Enzyme in glycogen phosphorylation
Phosphoproteins
27
PROSTHETIC GROUP -Nucleic Acid SPECIFIC EXAMPLE -Ribosomes -Viruses FUNCTION -Site for protein synthesis in cells Self-replicating, infectious complex
Nucleoproteins
28
PROSTHETIC GROUP -Metal Ion SPECIFIC EXAMPLE -Iron - ferritin -Zinc - alcohol dehydrogenase FUNCTION -Storage complex for iron -Enzyme in alcohol oxidation
Metalloproteins
29
PROTEIN CLASSIFICATION BASED ON SHAPE
1. FIBROUS PROTEINS 2. GLOBULAR PROTEINS
30
• These proteins are spiral and helical and are cross linked by disulphide and hydrogen bonds
FIBROUS PROTEINS
31
HIGH PROTEIN VEGETABLES (RANKED FROM HIGHEST TO LOWEST)
GREEN PEAS SPINACH ARTICHOKES CORN AVOCADO ASPARAGUS BRUSSELS SPROUTS MUSHROOMS KALE POTATOES
32
• They represent about 25-30% of all proteins among vertebrates.
Collagen
33
• 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.
Collagen
34
COLLAGEN RICH FOODS (FOR SKIN)
Berries Leafy Greens Citrus Fruits Nuts and Seeds Soy Products Tomatoes Avocado
35
COLLAGEN RICH FOODS (FOR SKIN)
Berries Leafy Greens Citrus Fruits Nuts and Seeds Soy Products Tomatoes Avocado
36
• 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 -Keratins
37
• 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.
Elastin
38
• Most of the proteins belong to this class, in which they have a compact and spherical structure and more complex than fibrous proteins.
GLOBULAR PROTEINS
39
They are generally soluble in water but can also be found inserted into biological membranes (transmembrane proteins). Hence, in a hydrophobic environment.
GLOBULAR PROTEINS
40
PROTEIN CLASSIFICATION BASED ON FUNCTION
Types: Enzymes Transport Structural Hormones Defence Contractile Storage
41
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.
Enzymes
42
EXAMPLES -Haemoglobin, Albumin FUNCTIONS -Carry substances in the blood or lymph throughout the body.
Transport
43
EXAMPLES -Actin, Tubulin, Keratin FUNCTIONS -Construct different structures like the cytoskeleton, hair, and nails.
Structural
44
EXAMPLES -Insulin, thyroxine FUNCTIONS -Coordinate the activity of different body systems
Hormones
45
EXAMPLES -Immunoglobulins (Antibodies) FUNCTIONS -Protect the body from invading pathogens
Defence
46
EXAMPLES -Actin, myosin FUNCTIONS -Effect of muscle contraction - for movement
Contractile
47
EXAMPLES -Legume storage of proteins, egg white (albumin) FUNCTIONS -Provide nourishment in early development of the embryo and the seedling.
Storage
48
IMMUNOGLOBULINS
IgA IgD IgE IgG IgM
49
Found in mucous, saliva, tears, and breastmilk Protects us against pathogens Transferred to an infant through breastmilk and colostrum.
IgA
50
Part of the B cell receptor - helps them to start the immune response. Activates basophils and mast cells
IgD
51
Protects against parasitic worms. Responsible for allergic reactions. Found mainly on tonsils, skin and mucous membranes.
IgE
52
Secreted by plasma cells in the blood Able to cross the placenta into the fetus - important in the immunity of newborn
IgG
53
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.
IgM
54
• 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.
Denaturation of Proteins
55
-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.
Denaturation of Proteins