Chapter Eleven : Vitamins and Proteins Flashcards

1
Q

Metabolism

A

Chemical processes that involve breaking down and building different substances in the body

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2
Q

What do carbs, fats and proteins hydrolyse to?

A

C- monosaccahrides
P - amino acids
F - glycerol and fatty acids

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3
Q

Minerals

A

Inorganic substances required in various amounts

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4
Q

Vitamins

A

Are a group of organic compounds that are essential for growth and nutrition, cannot be synthesised by the body

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5
Q

Proteins

A

For growth and repair of the cells, immunity and transport of molecules and as enzymes, hormones and structural components

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6
Q

Carbohydrates

A

To store and provide energy, for the functioning of the central nervous system and to remove waste from the body

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7
Q

Fat-soluble vitamins

A

A,D,E,K
Absorbed in the intestines
Stored as fat deposits in the lover
Mostly non-polar

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8
Q

Water soluble vitamins

A

Dissolve within the body as it is polar
8 different B groups and Vitamin C
Absorb directly into the bloodstream
Excreted through the kidneys in the urine
Must be obtained from food on a regular basis

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9
Q

Vitamin C - ascorbic acid

A

Maintains healthy immune system; assists in wound healing; helps the production of collagen
Red peppers, citrus, kiwi, broccoli

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10
Q

Roles of protein in the body

A
Acts as catalysts
Antibodies to prevent infection
Assist with formation of new molecules
Act as hormones
Provide structural components for cells
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11
Q

Amino acids

A

Monomers that contain amino and carboxyl groups

20 amino acids, 9 essential

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12
Q

Zwitterions

A

A dipolar ion containing equal positive and negative charges

A + charge goes on the N and a H is lost from COOH making it COO-

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13
Q

Zwitterions in acidic environment

A

Behaves as a base
Cationic form
Carboxyl groups combine with H+ to make uncharged COOH groups
Gives the ammonium ion a net pos charge of NH3+
<4 pH

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14
Q

Zwitterions in basic environment

A
Anionic form
Behaves as an acid
Ammonium group loses H+ - NH2
Carboxyl loses H+ becomes COO-
>8 pH
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15
Q

Formation of proteins

A

Amino acids combine to form peptides in a condensation reaction
A peptide is a reaction between NH2 and COOH with H2O as a product
May be fibrous (keratin, collagen) or globular (haemoglobin)

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16
Q

Structure of proteins

A

Primary structure - The order of amino acids which are covalently bonded in a polypeptide
Secondary structure - Hydrogen bonding causes the chain to coil, pleat or folds
Tertiary structure - Bonding between the side chains of the amino acids (h binding, dispersion, dipole dipole, Di sulfide, ionic)
Quatenary structure - When different protein molecules link together in a particular spacial arrangement

17
Q

Enzymes

A

Biological catalysts which lower the activation energy by providing an alternative pathway

18
Q

Difference between inorganic catalysts and enzymes

A

Inorganic catalysts
- speed up any reaction
Enzymes
- Very specific to what reaction they speed up

19
Q

Structure of enzymes

A

Enzymes have an active site which the substrate is manoeuvred to
Each shape of the active site is unique meaning it can only take 1 type of substrate

20
Q

Lock and key model

A

Molecules with complementary shapes fit into active sight and form a product

21
Q

Induced fit model

A

In the presence of a substrate the active site may change in order to fit the substrate’s shape
It will return to its original shape after being used

22
Q

Coenzymes

A

Are organic non-protein molecules that assist with the functioning of enzymes
Intermediate transporters of electrons

23
Q

Effect of temperature on enzymes

A

Each enzyme has optimal temp at body temp which is 37.5c if the temp exceeds this the enzyme will denature
If the temp goes under the reaction rate will slow down significantly but will not harm active site

24
Q

Effect of pH levels on enzymes

A

Each enzyme has a unique optimal pH if the pH is altered either above or below the enzyme will denature

25
Q

Denaturation

A

The collapse of intra and inter molecular bonds that maintain the shape in secondary, tertiary and quartenary structures of a protein
It alters the shape of the active site destroying catalytic activity

26
Q

Effect of concentration on enzymes

A

When the concentration of enzymes increase the rate of reaction increases proportionally
When concentration of substrates increase rate of reaction increases until a point of saturation as the active sites become saturated