2.1.2 Biological Molecules Flashcards

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1
Q

Biological molecules in a healthy diet

A
Carbohydrates 
Glucose
Protein
Water
Fibre
Iron
Fats and oils (lipids)
Vitamins and minerals
Nucleic acids
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2
Q

Carbohydrates are needed for…

A

Energy storage and supply, structure

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3
Q

Proteins are needed for…

A

Structure, transport, enzymes, antibodies, most hormones

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4
Q

Lipids are needed for…

A

Membranes, energy supply, thermal insulation, protective layers/padding, electrical insulation in neurones, some hormones

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5
Q

Vitamins and minerals are needed for…

A

Forming parts of larger molecules, take part in metabolic reactions, coenzymes or enzyme activators

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6
Q

Nucleic acids are needed as…

A

Information molecules that carry instructions for life

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7
Q

Water is needed to…

A

Take part in many reactions, support in plants, solvent/medium for most metabolic reactions, transport

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8
Q

Elements in biological molecules

A

Carbon
Hydrogen
Oxygen
Nitrogen

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9
Q

Metabolism

A

Rate of chemical reactions in your body that breaks down (catabolic) and builds up (anabolic) molecules

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10
Q

Monomers

A

Single molecules e.g. Amino acids

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11
Q

Dimer

A

Two monomers joined together

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12
Q

Polymer

A

More than 2 monomers joined together

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13
Q

Carbohydrates monomers and polymers are called..

A

Monosaccharides (simple sugars)

Polysaccharides

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14
Q

Proteins monomers and polymers are called..

A

Amino acids

Polypeptides and proteins

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15
Q

Nucleic acids monomers and polymers are called ..

A

Nucleotides

DNA and RNA

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16
Q

Condensation reaction

A

Chemical reaction that links biological monomers together with a covalent bond

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17
Q

Process of a condensation reaction

A

A water molecule is released
A new covalent bond is formed
A larger molecule is formed by the binding together of smaller molecules

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18
Q

Hydrolysis reaction

A

Splitting larger molecules into molecules

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19
Q

Process of a hydrolysis reaction

A

Water molecule is used
Covalent bond is broken
Smaller molecule is formed by splitting a larger molecule

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20
Q

Elements of carbohydrates

A

Carbon
Hydrogen
Oxygen C6H12O6
Make up 10% of the organic matter of a cell

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21
Q

Functions of carbohydrates

A
Energy source (glucose)
Energy store (starch and glycogen)
Structure (cellulose in plants, chitin in insects- held by exoskeleton)
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22
Q

For every carbon present in a carbohydrate….

A

The equivalent of a water molecule is also present

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23
Q

Monosaccharides

A

Monomers of carbs

Contain between 3-6 carbon atoms

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24
Q

Properties of monosaccharides

A

Soluble in water
Sweet tasting
Form crystals

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25
Q

Triose sugars

A

3 carbon monosaccharides

26
Q

Pentose sugars

A

5 carbon monosaccharides

E.g. Ribose C5H10O5

27
Q

Hexose sugars

A

6 carbon monosaccharides
Most common
Glucose and fructose

28
Q

Isomers

A

Different shaped forms of the same molecule

29
Q

Ribose

A

C5H10O5
Component of ribonucleic acid (RNA), ATP and NAD
Pentose sugar
monosaccharide (like glucose)

30
Q

Disaccharides

A

The joining of two monosaccharides

A new covalent bond, glycosidic bond forms and water is eliminated

31
Q

Examples of polysaccharides

A
Starch
Glucose
Cellulose
Amylose
Amylopectin
32
Q

Forming polysaccharides

A

Involves the making of glycosidic bonds

They are still sugars

33
Q

Benedicts test

A

Test for reducing sugars

34
Q

General formula for a carbohydrate

A

(CH2O)n

35
Q

qualititative tests

A

indicate only the type of molecule present, not how much is present

36
Q

polysaccharides as energy stores

A

glycogen in animals, starch in plants (amylose and amylopectin)

37
Q

similarities of starch and glycogen

A

energy stores, bonded by thousands of alpha molecules, glucose molecules in chains can be easily ‘broken off’, insoluble

38
Q

exoskeletons

A

polysaccharide chitin forms it in insects

39
Q

bacterial cell walls

A

polysaccharide peptigoglycan is the basis of cell walls found around most bacterial cells

40
Q

uses of proteins

A
growth and repair
enzymes
hormones
amino acids (monomer)
polypeptides
build muscle
meat
antibodies
ribosomes (protein synthesis)
carrier proteins eg. active transport, facilitated diffusion
41
Q

proteins

A

a diverse group of large and complex polymer molecules, made up of long chains of amino acids

42
Q

biological roles of proteins

A

structural: main component of body tissues
catalytic: all enzymes are proteins, catalysing many biochemical reactions
signalling: many hormones and receptors
immunological: all antibodies

43
Q

R group in amino acids

A

represents a side chain from the central alpha carbon atom

effects the types of bonds in tertiary structure

44
Q

peptide bonds

A

link two amino acids together to form a dipeptide in a condensation reaction

45
Q

polypeptide chains

A

when more amino acids are added to a dipeptide

46
Q

protease enzymes

A

breaking down proteins and polypeptides by formation and breakage of peptide bonds is catalysed by these enzymes

47
Q

bonds in tertiary structure of protein

A

disulphide: between cysteine aa, strongest
hydrogen: all levels
hydrophobic: between non-polar sections
hydrophillic: outside in globular proteins
ionic: sometimes carry a charge, form where oppositely charged aa are close to each other

48
Q

Quaternary structure

A

Refers to the fact that some proteins are made up of more than one polypeptide subunit joined together or a polypeptide and an inorganic component

49
Q

Lipids

A

A diverse group of chemicals that dissolve in organic solvents (alcohol) but not in water

50
Q

Role of hydrogen bonds in water

A

Network of bonds allows molecules to move around, continually breaking/making bonds. When water solid, bonds hold structure in semi-crystalline form that is less dense. Also restrict movement of water molecules in liquid water

51
Q

Why water molecules move less at lower temperature

A

Reduced kinetic energy and more hydrogen bonds form but don’t break so easily

52
Q

Cohesion

A

Property of water molecules sticking to each other when hydrogen bonds pull water molecules to surface

53
Q

Why water is an ideal transport medium in living organisms

A

Remains liquids over a large temperature range and can act as a solvent for many chemicals

54
Q

what type of group is the haem group

A

prosthetic group

55
Q

which parts of amino acids are involved in peptide bonds

A

amino group on one amino acid and carboxyl group on the other

56
Q

OH

A

hydroxyl group (needed in condensation/hydrolysis reactions)

57
Q

how glycosidic bonds between 2 monosaccharides are formed

A

condensation reaction

in maltose, bonds forms between carbon 1 on the first alpha glucose and carbon 4 so it is an alpha1-4 glycosidic bond

58
Q

breakdown of glycosidic bonds

A

hydrolysis reaction and molecule of water is added to break the bond

59
Q

why is haemoglobin a conjugated protein

A

it contains a prosthetic group- haem group is not essential and contains an iron ion

60
Q

how to test for reducing sugars commercially

A

test strips dipped into solution and compared to a chart indicating how much glucose present (often for urine from diabetic patients)