Biology 2.1.2 Flashcards

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1
Q

Protein

A

Diverse group of large complex polymers made up of chains of amino acids

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2
Q

Structural Protein

A

Main components of body tissue (skin, ligaments, hair)

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3
Q

Catalytic Proteins

A

Enzymes are proteins (catalyse chemical reactions)

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4
Q

Signalling Proteins

A

Proteins used in the functioning of the brain.

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5
Q

Immunological Proteins

A

Proteins responsible for communication between cells of the immune system.

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6
Q

What is the 3D shape in proteins maintained by?

A

Hydrogen Bonds, Hydrophobic interactions and Disulfide Bonds

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7
Q

Fibrous Proteins

A

formed from parallel polypeptide chains held together by crosslinks. (forms long rope-like fibres with high tensile strength and generally insoluble in water.

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8
Q

Collagen

A

the main component of connective tissue such as ligaments, tendons, cartilage

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9
Q

Keratin

A

the main component of hard structures such as hair, nails, claws and hooves.

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10
Q

silk

A

forms spiders’ webs and silkworms’ cocoons.

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11
Q

Globular proteins

A

have a spherical shape caused by tightly folded polypeptide chains. The chains are usually folded so that hydrophobic groups are on the inside and hydrophilic groups are on the outside, making many globular proteins soluble in water.

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12
Q

Transport Proteins

A

Proteins that are used to move other materials in an organism, such as Haemoglobin, myoglobin, and those embedded in membranes.

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13
Q

Enzymes

A

Biological catalysts such as lipase and DNA polymerase.

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14
Q

Hormones

A

Chemical messengers. Such as oestrogen and insulin.

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15
Q

Denatured Proteins

A

Bonds between proteins are broken due to changes in temperature, pH or salt concentration. Fibrous proteins lose structural strength when denatured whereas globular proteins become insoluble and inactive.

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16
Q

Test for Proteins and Positive result.

A

Biuret Reagent/ Test
Blue —>Lilac (positive result)

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17
Q

4 Structures of Proteins.

A

Primary
Secondary
Tertiary
Quaternary

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18
Q

What is the Primary Structure of Proteins?

A

multiple amino acids bound together via strong covalent peptide bonds to form a polypeptide chain.

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19
Q

What is the Secondary Structure of Proteins?

A

Localized structures that form based on interactions within the protein backbone(what holds a protein together and gives it an overall shape).
Alpha helix or beta pleated sheet.
Has hydrogen bonds between coils of the same chain.

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20
Q

What is the Tertiary Structure of Proteins?

A

The overall three-dimensional arrangement of its polypeptide chain in space.

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21
Q

What is the Quaternary Structure of Proteins?

A

association of several protein chains or subunits into a closely packed arrangement.

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22
Q

Polypeptide

A

A peptide consisting of 2 or more amino acids.

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23
Q

What is the ‘R Group’?

A

The R group is a side chain from the central ‘alpha’ carbon atom that defines an amino acid.

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24
Q

What is cohesion and why is water cohesive?

A

Water molecules stick to each other due to the hydrogen bonds.

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25
Q

Role of the cohesion of water in survival

A
  1. Allows water to form continuous stream which benefits plants intake of water through the xylem.
  2. Also creates surface tension which resists force allowing some organisms to walk on top.
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26
Q

Why does water have a high specific heat capacity and a high latent heat of vaporisation?

A

Strong Hydrogen bonds require lots of energy to overcome.

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27
Q

Role of the high specific heat capacity of water in survival.

A

Stabilises communities since water temperatures don’t change by much.
Links to homeostasis and enzymes.

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28
Q

Role of high latent heat in survival

A

Allows us to maintain our temperature by cooling off through sweating.
Links to homeostasis.

29
Q

Why is water a good solvent?

A

Water is polar so it allows water to bind to solute molecules.

30
Q

Roles of water as a solvent in survival

A

Medium for reactions
Transport (circulatory system- blood)
Dissolves minerals and gases and ions
Dilutes toxic substances.

31
Q

Elements found in carbohydrates

A

Carbon, hydrogen, oxygen

32
Q

Elements found in lipids

A

Carbon, hydrogen and oxygen

33
Q

Elements found in proteins

A

Carbon, hydrogen, oxygen, nitrogen, sulfur

34
Q

Elements found in Nucleic acid.

A

Carbon, hydrogen, oxygen, nitrogen, phosphorus.

35
Q

Cations involved in biological processes.

A

Calcium, ammonium, potassium, hydrogen, sodium.

36
Q

Anion involved in biological processes.

A

Hydroxide, chloride, hydrogen carbonate, phosphate, nitrate.

37
Q

Metabolism

A

Rate of all chemical reactions in an organism.

38
Q

Condensation

A

Formation of a bond with the release of water(2 -OH groups)

39
Q

Hydrolysis

A

Breaking bonds with the addition of water.

40
Q

Simple Carbohydrates

A
  1. Monosaccharides (monomers)
    E.g. glucose
  2. Disaccharides (polymers)
    E.g. sucrose
41
Q

Complex carbohydrates

A

Polysaccharides (polymers)
E.g. Starch.

42
Q

Carbohydrates general formula

A

Cx(H2O)y

43
Q

Lipids

A

Diverse group of compounds that are insoluble in water but soluble in organic solvents like ethanol.

44
Q

What’s ABBA?

A

-OH on C1on glucose
Alpha
Below
Beta
Above.

45
Q

Why is glucose soluble?

A

Glucose forms hydrogen bonds with water.

46
Q

Ribose vs Glucose

A

Glucose is a hexose sugar (6 carbons)
Ribose is a pentose sugar (5 carbons)

47
Q

Galactose

A

Not as soluble as glucose but is used in the production of glycoproteins and glycolipids. -OH and H in C4 of glucose is switched.

48
Q

Fructose

A

Very soluble and is the main sugar in fruits and nectar, it is sweeter than sugar.CH2OH in C1 of Ribose instead of H.

49
Q

Deoxyribose

A

Has no O on C2 of ribose.

50
Q

Formation of disaccharides

A

1.Condensation reaction forming a glycosidic bond.

51
Q

Monosaccharides that make up :
1.Maltose
2.Sucrose
3.Lactose

A
  1. Glucose and Glucose
  2. Glucose and Fructose
  3. Glucose and Galactose
52
Q

(x,y) glycosidic bond.
What is ‘x’ and ‘y’?

A

x= which numbered carbon the compound on the left is bonding
y= which numbered carbon the compound on the right is bonding.

53
Q

Test for reducing sugars

A
  1. Add Benedicts reagent
  2. Heat to 60-80°C
  3. A positive result is blue ——> green/yellow/orange/brown/red.
54
Q

Test for non-reducing sugars

A
  1. Hydrolysis
  2. Boil with HCl and neutralize
  3. Add Benedicts reagent
55
Q

Isomer

A

Compounds with the same chemical formula but different structure.

56
Q

Reducing sugar

A

Sugars that are capable of being reducing agents (brings reduction).

57
Q

Polysaccharides

A

Multiple monosaccharides bound together with glycosidic bonds.
Mainly used as an energy store and a structural component of cells.

58
Q

Properties of starch

A

Easily compacted
Insoluble
Few branches (slow release of energy)
Hydrolysed by amylase into glucose for energy.

59
Q

Amylose

A

-Made from chains of alpha glucose bound together by 1-4 glycosidic bonds. This chain forms a helix (6 units of glucose per turn).
-Insoluble in water.

60
Q

Amylopectin

A

Made up of alpha glucose bonded by 1-4 and 1-6 glycosidic bonds forming branching chains. This structure also coils
Insoluble in water

61
Q

Test for starch

A

Iodine test
Positive result: Brown—->blue black

62
Q

Cellulose

A

Composed of beta glucose, where each glucose molecule is rotated 180° and bonded with beta glycosidic bonds. Each adjacent parallel chain is held together by hydrogen bonds giving cellulose structural strength.
It’s Insoluble in water.

63
Q

Glycogen

A

Animals store glycogen.
Very similar to amylopectin but has more branches, meaning it can be broken down faster for more energy (respiration).
Forms 1-4 and 1-6 alpha glycosidic bonds.
Coils.

64
Q

Lipid functions:

A

Protection
Energy source
Buoyancy
Insulation
Waterproofing

65
Q

What are the bonds between fatty acids and the glycerol.

A

Ester bonds

66
Q

Saturated vs Unsaturated

A

No C=C bond means it is saturated, more fluid.

67
Q

Phospholipid

A

Has a phosphate in the hydrophilic head, with only 2 hydrophobic non polar fatty acid tails.

68
Q

Cholesterol

A

Absorbed by food and can be synthesised.
Stabilises and regulates the fluidity of membranes.