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Biology AS > Biological Molecules, 2.2 > Flashcards

Biological Molecules, 2.2 Flashcards

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1
Q

What are the main elements that make up life?

A

Carbon, hydrogen, oxygen, nitrogen, lipids, nucleic acid

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2
Q

What is the metabolism?

A

Total of all chemical reactions which occur in the body

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3
Q

Anabolic

A

Uses energy to build

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4
Q

Catabolic

A

Uses to energy to break

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5
Q

What is a monomer? And an example?

A

Single small molecule. Amino acids, monosaccharides and nucleotides.

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6
Q

What is a polymer? And an example?

A

Many monomers joined in a long chain. Proteins, polysaccharides and DNA.

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7
Q

Define a covalent bond.

A

Two non-metals share electrons to achieve a full outer shell.

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8
Q

What is a condensation reaction?

A

Chemical reaction linking biological monomers together. Water molecule is released. Covalent bond is formed.

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9
Q

What is a hydrolysis reaction?

A

Splits larger into smaller. Water molecule is used. Covalent bond is broken.

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10
Q

What is hydrogen bonding?

A

Oxygen molecule slightly negative. Hydrogen molecule slightly positive. Molecule is polar. Forms a weak interaction. Stabilizes a structure.

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11
Q

What are some of the uses of water?

A

Provides habitats eg lakes and oceans. Major component of tissue. Reaction medium for chemical reactions. Effective transport medium.

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12
Q

What are the advantages of water density?

A

Ideal for living things able to float. Less dense in its solid form - organisms live underneath. Ice insulates the water.

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13
Q

Why is water a good solvent?

A

Polar molecule - can pull apart molecules with charges involved. Provides a place for reactions.

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14
Q

Why does water have properties of cohesion and surface tension?

A

Hydrogen bonding means molecules pull together. Creates surface tension. Water contracts - gives the surface the ability to resist force applied.

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15
Q

What does high specific heat capacity mean?

A

When lots of hydrogen bonds combine it takes a lot of heat to increase their kinetic energy. High latent heat of vaporization. 1Kg by 1degrees = 4.2kJ

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16
Q

How does water provide support?

A

Cells remains turgid. Vacuole - water moves in. Hydrostatic skeleton.

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17
Q

What are some examples of carbohydrates?

A

Triose sugars (3C) - glyceraldhyde. Pentose sugars (5C) - ribose and deoxyribose. Hexose sugars (6C) - glucose and fructose.

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18
Q

What is the difference between alpha and beta cells?

A

The position of OH attached to carbon 1. Alpha Below Beta Above - ABBA.

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19
Q

What polymers do alpha glucose form?

A

Animals - glycogen. PLants - starch (amylose).

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20
Q

What polymers do beta glucose form?

A

Cellulose - cannot be broken down.

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21
Q

Give three examples of Dissacharides and what they are made from?

A

Maltose - alpha + alpha. Sucrose - alpha + fructose. Lactose - B galactose + alpha.

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22
Q

What is the bond that forms between monosaccharides and which carbons is it between?

A

Glycosidic bond. Between carbon 1 and carbon 4. Bond between OH groups.

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23
Q

What is a reducing sugar?

A

An oxidising agent. Loses an electron. Donates to another molecules.

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24
Q

How do you do a test for a reducing sugar?

A
  1. Add a Benedicts reagent - blue copper (II) ions (CU2+).
  2. The sugar will donate electrons to the Benedicts reagent.
  3. Cu+ is soluble in water so will turn to a brown/red precipitate
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25
Q

How do you do a test for a non-reducing sugar?

A
  1. Add hydrochloric acid to the sugar to break the bonds down into glucose.
  2. Sodium hydrogen carbonate is added to neutralise the acid.
  3. Proceed with the reducing sugar test as normal.
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26
Q

What are the main features of glycogen?

A

Compact. Chains and branched - glucose can be accessed quickly. 1-4 and 1-6 glycosidic bonds. Insoluble. Store of glucose.

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27
Q

What are the main features of amylopectin?

A

Branched chains - glucose picked off the ends. 1-4 and 1-6 glycosidic bonds. Coils into spirals. Energy store.

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28
Q

What are the main features of amylose?

A

1-4 glycosidic bonds. Coils into a spiral. Long chain. Insoluble. Storage.

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29
Q

What is starch made up from?

A

Amylopectin and amylose.

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30
Q

What are the main features of cellulose?

A

In cell walls. Strong - prevents cells bursting. Chain of beta glucose. 1-4 glycosidic bonds. Rope like microfibrils. Every second B glucose is rotated 180 degrees. Unbranched.

31
Q

How do you measure the amount of glucose?

A

The more glucose present the more precipitate formed - can be measured with a colorimeter. Produce a calibration curve.

32
Q

What are the different types of proteins?

A

Structural (body tissues). Enzymes. Hormones (signalling). Antibodies (immunological).

33
Q

What is the structure of an amino acid?

A

Amino group (NH2). Carboxyl group (COOH). R group (element differs).

34
Q

How do amino acids act as buffers?

A

In water the amino group and carboxyl group ionise. Carboxyl group acts as an acid. Amino group acts as a base.

35
Q

What bonds are amino acids joined by and what is the bond between?

A

Peptide bond. Carbon and Nitrogen.

36
Q

Why is the structure of a protein important?

A

For signalling, structure and receptors.

37
Q

What is the primary structure of a protein?

A

Order of amino acids. Order affects the overall shape and determines function.

38
Q

What is the secondary structure of a protein?

A

Amino acid chain twists in an alpha helix. Held by hydrogen bonds. B gluocse folds into a zig zag froming a B pleated sheet.

39
Q

What is the tertiary structure of a protein?

A

Coils and pleats fold themselves into a precise shape. Held in place by amino acids bonding.

40
Q

What is the quaternary structure of a protein?

A

Multiple polypeptide chains arranged. Held in place by bonds.

41
Q

What is ionic bond and what are the bonds between in proteins?

A

Transfer of electrons, strong electrostatic attraction between ions. Between carboxyl and amino groups that are part of R groups.

42
Q

What are disulfide bonds and what are they between in proteins?

A

Strong covalent bonds. R group of cysteine contains sulfur between two cysteines.

43
Q

What are hydrophobic and hydrophillic interactions and what are they between in proteins?

A

R groups tend to associate together. Causes twisting of the chain.

44
Q

What are some examples of fibrous proteins? And key features?

A

Collagen. Keratin. Elastin. They are insoluble and form fibres.

45
Q

What are the main features of collagen?

A

Mechanical strength. Rope like chains. Covalently bonded. Connective tissue. Artery walls, tendons and bones.

46
Q

What are the main features of keratin?

A

Mechanical strength. Impermeable barrier to infection. Disulfide bonds. Hair and nails.

47
Q

What are the main features of elastin?

A

Strong and extensible. Coiling and cross linking. Skin stretch over bones. Allows lungs to inflate and deflate. Blood vessels.

48
Q

What are some examples of globular proteins? And key features?

A

Spherical shape. Hydrophobic - inside. Hydrophillic - outside. Soluble in water. Transport, Enzymes and Hormones.

49
Q

What are the main features of haemoglobin?

A

Oxygen away from lungs to tissue. Oxygen binds to iron in each of the haem groups.

50
Q

What are the main features of insulin?

A

Two chains joined by disulfide bonds. Cause cells to increase glucose uptake. Binds to glycoprotein receptors.

51
Q

What are the main features of pepsin?

A

Digests protein in the stomach - catalyses breakdown. Single chain which folds. Only a few amino acids. 43 acidic R groups.

52
Q

How do we test for proteins?

A

Biuret test. Colour changes from blue to lilac. Complex formed between nitrogen and Cu2+ ions.

53
Q

How does chromatography work?

A

Separates a mixture. Exposed OH groups make the surface polar, allows it to form dipole interactions

  1. Draw a line
  2. Spot the mixture on the line
  3. Dip the bottom of the paper in solvent
  4. Solvent travels up the paper taking substances from the mixture with it
  5. Substances travel at different speeds and end up in different positions
54
Q

What is the stationary phase?

A

Chromatography paper or TLC plate.

55
Q

What is the mobile phase?

A

Solvent eg water or ethanol.

56
Q

What is the Rf value?

A

x/y. x = line to pigment spot. y = line to solvent front.

57
Q

What would you have to use to be able to see the pigment spots on the TLC?

A

UV light. Ninhydrin. Iodine.

58
Q

What are the key features of lipids?

A

Energy source. Mostly C and H. Insoluble as they’re not polar.

59
Q

What are triglycerides made up of?

A

Glycerol (C,H, O) and fatty acids (COOH).

60
Q

What is the structure of glycerol?

A

3C. Alcohol. 3 OH groups - fatty acids bond to.

61
Q

What is the structure of a fatty acid?

A

Carboxyl group (COOH) - ionises to H+ and COO-. Saturated C=C.

62
Q

What are the functions of a triglyceride?

A

Energy source, releases ATP. Energy store, store fat in adipose. Insulation, storage in whales. Buoyancy, fat less dense than water. Protection.

63
Q

What is the bond between glycerol and fatty acids and what molecules is it between?

A

Ester bond. Between COOH and OH.

64
Q

What is the structure of a phospholipid?

A

Glycerol. 2 fatty acids. Phosphate group.

65
Q

What are the functions of a phospholipid?

A

Phosphate - polar - hydrophillic. Fatty tails - non polar - hydrophobic. Form micelles. Form phospholipid bilayer - tails inwards, heads outwards. Membrane is selectively permeable.

66
Q

What is the structure of cholesterol?

A

Steroid alcohol. 4 carbon based rings.

67
Q

What is the function of cholesterol?

A

Sits in the hydrophobic part of the bilayer. Regulates fluidity. Small. Hydrophobic. Made in the liver. Testosterone and oestrogen.

68
Q

How does an emulsion test work?

A
  1. Add ethanol to lipid sample - shake it
  2. Ethanol is non-polar - lipids won’t dissolve
  3. Add to water where it won’t dissolve - cloudy white emulsion will form.
69
Q

Examples of cations.

A

Ca2+. Na+. K+. H+. NH4+.

70
Q

Examples of anions.

A

NO3-. HCO3-. Cl-. PO3-. OH-.

71
Q

What is different of lipid content in microorganisms than in animals?

A

Less overall fat/lipid. Less/no saturated fat. More unsaturated fat.

72
Q

What is the structure of a collagen?

A
  1. Peptide bonds between amino acid
  2. Every 3rd amino acid is glycine
  3. Coils
  4. Left handed helix
  5. Three polypeptide chains
  6. Hydrogen bonds between chains
  7. No hydrophilic groups on the outside
  8. Cross links - joined adjacent molecules
  9. Fibril
73
Q

What is the structure of haemoglobin?

A
  1. Globular
  2. 4 chains
  3. Alpha helix
  4. Hydrophobic groups on the inside
74
Q

How does TLC work?

A
  • Uses silica gel
  • Separates by solubility
  • Separates by non charged molecules
  • Can use dyes

Biology AS (12 decks)

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