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Biology A-Level OCR > Biological Molecules > Flashcards

Biological Molecules Flashcards

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1
Q

What roles do ions have in biological systems?

A

Cell shape, involved in enzymic catalyst, chromosome shape, muscle contactions

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2
Q

What is the function of Ca2+

A

Nerve impulse, muscle contractions

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3
Q

What is the function of K+

A

Nerve impulse, stomal opening

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4
Q

What is the function of NH₄+

A

Production of nitrate by bacteria, nitrogen source, nitrogen waste component

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5
Q

What is the function of Na+

A

Nerve impulse, kidney function

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6
Q

What is the function of H+

A

Cataylsis of reactions, pH determination

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7
Q

What is the function of NO3-

A

Nitrogen supply to plants for amino acids, protein formation

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8
Q

What is the function of Cl-

A

Balance of other ions in cells

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9
Q

What is the function of OH-

A

Catalysis of reactions, pH determination

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10
Q

What is the function of HCO3-

A

Maintenance of blood pH

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11
Q

What is the function of PO4 3-

A

Cell membrane formation, nucleic acid formation, ATP formation, bone formation

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12
Q

What shape does water have and why?

A

Bent, non-linear shape because The oxygen molecules is slightly negative and the hydrogen molecules are slightly positive therefore the positive charges between the hydrogen molecules repel

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13
Q

What is the symbol for slightly?

A

δ Delta

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14
Q

What is meant by the term polar?

A

A polar molecule is a molecule that has both positive and negative charges

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15
Q

What is cohesion?

A

When the same molecules are attracted to each other due to its polarity

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16
Q

What effect does cohesion have on the melting and boiling point of molecules?

A

It increases as more energy is required to break the bonds between the molecules

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17
Q

What is a condensation reaction?

A

A reaction when monomers form to become larger units and a water molecule is formed from the forming of the hydroxyl group and the hydrogen ion

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18
Q

What is a hydrolysis reaction?

A

A reaction when water molecules are used to break up larger molecules into smaller ones

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19
Q

What is the general formula of a carbohydrate?

A

(CH2O)n (n = between 3-8)

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20
Q

What is the name of a carbohydrate with 3 carbons in the backbone?

A

Trisose

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21
Q

What is the name of a carbohydrate with 5 carbons in the backbone?

A

Pentose

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22
Q

What is the name of a carbohydrate with 6 carbons in the backbone?

A

Hexose

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23
Q

What is an Aldehyde group

A

H-C=O

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24
Q

What is the formula of glucose?

A

(CH2O)6

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25
Q

What is the difference between alpha and beta glucose?

A

The placement of the hydroxyl group, isomerism

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26
Q

What are some properties of glucose?

A

Small, soluble, strong due to bonds, easily bonds to each other for storage

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27
Q

What are some of the differences between amylose and amylopectin?

A

Amylose is unbranched and coiled whereas amylopectin is branched.

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28
Q

What are some similarities between amylose and amylopectin?

A

Both have alpha glucose as a monomer

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29
Q

What is the difference between amylopectin and glycogen?

A

Amylopectin is a part of starch and is glucose storage in plants but glycogen is glucose storage in animal and fungal cells

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30
Q

What is a reducing sugar?

A

A monosaccharide or disaccharide have a Ketone or Aldehyde group with ‘free’ electrons

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31
Q

What is a non-reducing sugar?

A

A sugar that cannot donate electrons

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32
Q

What is the test for reducing sugars?

A

Benedict’s reagent with sample in warm water

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33
Q

What is a positive result for Benedict’s test?

A

Solution goes brick red

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34
Q

Why does the colour change in a Benedict’s test?

A

Because electrons are donated to the Cu2+ in solution, which forms red Copper Oxide

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35
Q

What is a negative result for Benedict’s test?

A

Solution remains blue

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36
Q

What is the test for non-reducing sugars?

A

Add hydrochloric acid, heat in water bath, allow to cool, neutralise with sodium hydrogen bicarbonate, then repeat Benedict’s test

37
Q

What is the test for starch?

A

Iodine

38
Q

What is a glycosidic bond?

A

A type of covalent bond that bonds a carbohydrate to another group (which may or may not be another carbohydrate)

39
Q

What is the enzyme that digests starch?

A

Salivary and pancreatic amylase

40
Q

What is the enzyme that digests glycogen?

A

Beta cells in pancreatic islets secrete glucagon which activates enzymes that digest glycogen

41
Q

What is the enzyme that digests cellulose?

A

Cellulase

42
Q

Give an example of a reducing sugar

A

Glucose, fructose

43
Q

Give an example of a non-reducing sugar

A

Sucrose

44
Q

Name the three main lipid types

A

Triglycerides, phospholipids and cholesterole

45
Q

What are the subunits of triglycerides?

A

3 Fatty acids and glycerol

46
Q

How are triglycerides formed?

A

Condensation reactions, 3 water molecules released in esterification

47
Q

What is the triglyceride structure?

A

Hydrophilic base with 3 hydrophobic tails

48
Q

What are unsaturated fats?

A

Liquid fats with double bonds between carbon atoms

49
Q

What are saturated fats?

A

Solid fats with no double bonds between the carbon atoms

50
Q

What is the variable in amino acids?

A

The R group

51
Q

What are the subunits of phospholipids?

A

Phosphate group and 2 fatty acids

52
Q

Phospholipids are surfactants. What does this mean?

A

Surfactants are molecules that lower surface tension

53
Q

What do phospholipids make up?

A

Cell membranes- phospholipid bilayer

54
Q

What are the differences between phospholipids and triglycerides?

A

Triglycerides have 3 fatty acids tails, phospholipids have 2 fatty acid tails
Triglycerides do not have a phosphate group base

55
Q

What is the structure of cholesterol?

A

4 steroid rings with a hydrocarbon tail, thin

56
Q

Why is cholesterol both hydrophobic and hydrophillic?

A

Because the hydroxyl group is attracted to water but the steroid rings and hydrocarbon tail repel from water

57
Q

What is cholesterol insoluble in?

A

Human blood

58
Q

How does the structure of cholesterol help the structure of animal cell membranes?

A

The small, thin structure allows cholesterol to fit inbetween the phospholipid bilayer and maintain the temperature of fluids inside the cell by changing the fluidity of the cell membrane

59
Q

State and describe the tests for lipids

A

Emulsion test: add ethanol and water to sample, shake solution and observe

60
Q

What is a positive result for a lipids test?

A

The solution will go cloudy

61
Q

What is used in a quantitative sugars test?

A

A colourimeter

62
Q

What are proteins?

A

A molecule containing 2 or more polypeptides joined together

63
Q

What are polypeptides?

A

A polypeptide is 2 or more amino acids joined together by peptide bonds

64
Q

What are the components of an amino acid?

A

An amine group, hydrogen, a central carbon, an R group variable, a carboxyl group, covalent bonds

65
Q

What are the four structures of proteins?

A

Primary, secondary, tertiary and quaternary

66
Q

What is the primary structure of proteins?

A

Simple chain of amino acids, only has peptide bonds, no R-group interactions

67
Q

What is the secondary structure of proteins?

A

Alpha helix or beta-pleated sheet, only has hydrogen and peptide bonds, no R-group interactions, 3D

68
Q

What is the tertiary structure of proteins?

A

Long chain, ionic, disulfide, hydrogen and peptide bonds, hydrophilic and hydrophobic interactions, R-group interactions, may have prosthetic groups, 3D

69
Q

What is the quaternary structure of proteins?

A

Multiple protein subunits (jumbled mess), maybe alpha and beta chains, ionic, disulfide, hydrogen and peptide bonds, hydrophilic and hydrophobic interactions, 3D

70
Q

What are the different types of proteins?

A

Globular, conjugated and fibrous

71
Q

Name the features of globular proteins

A

Tertiary shape, compact, water-soluble, spherical

72
Q

What are some functions of globular proteins?

A

Immunity, muscle contraction, chemical reactions

73
Q

Name an example of a globular protein

A

Insulin

74
Q

How do the properties of globular proteins affect insulin’s function?

A

Transported via blood so needs to be soluble, needs to fit onto cell receptors so needs to be a specific shape

75
Q

Name the features of conjugated proteins

A

Globular with a non-amino acid component

76
Q

What are prosthetic groups?

A

Non-amino acid component (R-group)

77
Q

What are proteins called if they don’t have prosthetic groups?

A

Simple proteins

78
Q

What are some possible prosthetic groups of conjugated proteins?

A

Lipids (lipoproteins), carbohydrates (glycoproteins), metal ions, molecules

79
Q

Name two examples of conjugated proteins

A

Haemoglobin, catalase

80
Q

How are the properties of haemoglobin affected by its prosthetic group?

A

Iron II, quaternary protein with 2 alpha and 2 beta subunits, iron II bonds reversibly with oxygen so good for transport

81
Q

How are the properties of catalase affected by its prosthetic group?

A

An enzyme, quaternary, prosthetic group of iron II, breaks down hydrogen peroxide which is useful because it is damaging to cells (a common byproduct of metabolic processes)

82
Q

Name the features of fibrous proteins

A

Primary structure, long, strong, repetitive, limited and usually small R-groups, insoluble, organised, simple, NOT COMPLEX OR 3D!!!

83
Q

Name three examples of fibrous proteins

A

Keratin, elastin and collagen

84
Q

Name some features of keratin

A

Group of fibrous proteins present in hair, skin and nails, contains lots of cysteine which results in lots of disulfide bonds which makes keratin strong, inflexible and insoluble

85
Q

What does the flexibility of fibrous proteins depend on?

A

The angle of the disulfide bonds

86
Q

Name some features of elastin

A

Makes up elastic fibres in walls of blood vessels and alveoli in the lungs, give structure and flexibility so can expand if needed, quaternary protein made of TROPOELASTIN

87
Q

What is tropoelastin?

A

Subunit of elastin that is able to stretch and recoil without breaking, has alternate hydrophobic and lysine-rich areas

88
Q

Name some features of collagen

A

Connection tissue found in skin, tendons, ligaments and the nervous system, made of three polypeptides wound together into a triple helix (strong rope-like structure)

Biology A-Level OCR (26 decks)

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