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Unit 1: Biological Molecules > Carbohydrates, Proteins, Lipids, Enzymes > Flashcards

Carbohydrates, Proteins, Lipids, Enzymes Flashcards

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Organic Chemistry 101 flashcards
1
Q

What elements do carbohydrates contain and in what ratio?

A

Carbon, hydrogen, oxygen

2 hydrogen: 1 oxygen

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2
Q

What three groups can carbohydrates be classified into?

A

MONOsaccharides, eg. Glucose

DIsaccharides, eg. Sucrose

POLYsaccharides, eg.

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3
Q

What do monosaccharides and disaccharides have in common?

A

Small, soluble molecules
Easy to transport
Sweet to taste

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4
Q

Give three examples of simple sugars?

A

Monosaccharides
Disaccharides
Polysaccharides

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5
Q

What are the basic monomers of carbohydrates?

A

Monosaccharides

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6
Q

What are monosaccharides mainly used for?

A

Provide energy in respiration
In growth during the formation of larger carbohydrates

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7
Q

Three examples of monosaccharides?

A

Glucose
Fructose
Galactose

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8
Q

What’s the formula of monosaccharides?

A

C6 H12 O6

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9
Q

What result will the monosaccharides, glucose, fructose and galactose give in Benedict’s test?

A

Red brick colour as all reducing sugars

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10
Q

What’s the structure of a-glucose?

A
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11
Q

What’s an isomer?

A

Structural isomers are molecules with the same molecular formula but a different structural formula.

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12
Q

What’s the formula of disaccharides?

A

C12 H22 O11

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13
Q

When is a disaccharide formed?

A

Two monosaccharides joined together by a glycosidic bond in condensation reaction

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14
Q

What’s a condensation reaction?

A

Smaller molecules (monosaccharides) join together to form a larger molecule (disaccharide) with the release of water

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15
Q

Give three examples of disaccharides?

A

Maltose
Sucrose
Lactose

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16
Q

How is maltose formed?

A

Condensation of two glucose molecules

glucose + glucose = maltose + water

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17
Q

How is sucrose formed?

A

Condensation of a glucose molecule and fructose molecule

Glucose + Fructose = Sucrose + Water

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18
Q

How is lactose formed?

A

Condensation of a glucose and galactose molecule

glucose + galactose = lactose + water

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19
Q

What type of bond is a glycosidic?

A

Covalent bond

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20
Q

What’s an hydrolysis reaction?

A

Lysis (breakdown) of a larger molecule (disaccharide) into smaller molecules (monosaccharides) by the addition of water

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21
Q

How can disaccharides be hydrolysed?

A

Boiling with acid, eg. Dilute HCL
Heating with an enzyme at an optimum temp

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22
Q

What elements do lipids contain? (Proportions to carbohydrates?)

A

-Carbon, hydrogen and oxygen
-lower proportion of oxygen and higher proportion of hydrogen compared to carbs

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23
Q

What’s the function of lipids?

A

-used in respiration
-as structural and storage molecules

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24
Q

What are triglycerides?

A
  • consist of fats (solid) and oils (liquid) at room temp
    -insoluble in water
    -soluble in a range of organic solvents eg. Alcohol
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25
Q

Why are triglycerides ideal storage compounds?

A
  • yield twice as much energy as carbohydrates when fully oxidised (respired)
  • insoluble so osmotically inactive
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26
Q

How are triglycerides formed?

A

-Joining 3 fatty acids to 1 glycerol molecule
-during condensation reaction with the loss of 3 water molecules

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27
Q

What is the general formula of a fatty acid?

A

-R-COOH
-R= long hydrocarbon chain
-COOH= carboxylic acid group

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28
Q

Describe a saturated fatty acid.

A

-no double bonds between carbon atoms
-straight chain
-contains the most amount of hydrogen molecules it can
-bad fats (eg. Butter)

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29
Q

Describe an unsaturated fatty acid.

A

-contain one or more double bonds between carbon atoms
-kinky structure
-kinks give it an oily texture
-good fats (eg. Oils)

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30
Q

What’s the structure of glycerol?

A
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31
Q

What’s the bond formed between glycerol and a fatty acid in a condensation reaction?

A

Ester bond

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32
Q

How can lipids be hydrolysed?

A

-heating with acid or alkali
-using lipase enzyme at an optimum temperature and pH

33
Q

How can you test for lipids?

A

Emulsion test

34
Q

Describe the emulsion test for lipids.

A

-small amount of sample in a test tube with 2cm^3 of ethanol
-shake mixture so fat dissolves
-add to water in another test tube and mix
-a white or cloudy emulsion of fat droplets indicates lipid is present

35
Q

What is a phospholipid?

A

A lipid containing a phosphate group.
(Phospholipid replaces one of the fatty acid molecules)

36
Q

What does a phospholipid consist of?

A

-1 glycerol
-2 fatty acids
-A phosphate group joined in a condensation reaction

37
Q

Explain the structure of a phospholipid.

A

-has a phosphate polar hydrophilic head
-two fatty acid non-polar hydrophobic tails

38
Q

What happens when a thin layer of phospholipids are in contact with water?

A

-forms a single layer of
-hydrophilic heads are attracted to the water
-hydrophobic tails repel the water and project outwards

39
Q

Where is a bilayer found?

A

Cell membrane

40
Q

What’s a bilayer?

A
  • two layers of phospholipids
    -hydrophobic tails are attracted to each other and repel the water
41
Q

What’s the function of cholesterol in a bilayer?

A

-cholesterol inbetween phospholipids
-increases stability of plasma
-makes it less flexible

42
Q

How does a bilayer effect permeability of the membrane?

A
  • gives membrane selective permeability
  • select what they allow to go through the cell membrane
43
Q

Why would red blood cells have a higher percentage of cholesterol than cell lining?

A

-red blood cells have no support so need lots of cholesterol
-cells lining walls have supports and stability from the cells around them

44
Q

What does protein contain?

A

-carbon
-hydrogen
-oxygen
-nitrogen
-sometimes sulphur

45
Q

What’s the monomer of proteins?

A

Amino acids

46
Q

What is the structure of an amino acid?

A

-amino group (NH2)
-carboxylic acid group (COOH)
-differ in the atomic group R

47
Q

What is the bond between two animo acids?

A

A peptide bond (-CONH-) formed by condensation reactions

48
Q

What do two animo acids joined together form?

A

Dipeptide

49
Q

What does many animo acids joined together form?

A

Polypeptide

50
Q

How can proteins be hydrolysed?

A

-heating with acid
-using enzyme (protease) at its optimum temp

51
Q

What’s the primary structure of a protein?

A

-sequence of animo acids joined by peptide bonds in a polypeptide chain
-this sequence determines the specific shape of the protein and where bonds form which determines specific 3D shape

52
Q

What is the secondary structure of a protein?

A

-the PLEATING or COILING of the polypeptide chain
-as a result of hydrogen bonding between amino acids
-inc: helix, b-pleated sheet

53
Q

What is the tertiary structure of a protein?

A

further folding and coiling of the secondary structure due to:
-hydrogen bonds
-peptide bonds
-ionic bonds (between + and - R-groups)
-disulfide bonds (between different R-groups)

54
Q

What does the tertiary structure of an enzyme determine?

A

The shape of its active site and its precise function

55
Q

Draw a disulfide bridge

A
56
Q

Draw a peptide bond

A
57
Q

Draw an ester bond

A
58
Q

Draw a glycosidic bond

A
59
Q

What happens if you change the sequence of amino acids?

A

-causes mutations
-could change shape of active site
-causing enzyme to be non-functional or have a different function

60
Q

What are Gobular proteins?

A

-consist of a highly folded and coiled polypeptide chain/chains
-produce a compact, complex tertiary structure
-include enzymes and antibodies
-soluble
-have specific tertiary structure

61
Q

What are fibrous proteins?

A

-typically long, thin and insoluble
-have structural functions eg. Keratin in hair, collagen in connective tissues

62
Q

What’s the quaternary structure?

A

highly complex proteins consisting of more than one polypeptide chain. Eg. Adult haemoglobin consists of four polypeptide chains

63
Q

What bonds hold together a quaternary structure?

A

-ionic
-hydrogen
-disulfide bridges
-hydrophobic interactions

64
Q

What’s the denaturation of proteins?

A

-alteration in the tertiary structure of a protein
-loss of 3D shape is often irreversible and protein is no longer functional

65
Q

What causes the denaturation of proteins?

A

-breaking of hydrogen and ionic bonds
-can be caused by high temps above optimum, extreme changes in pH and by heavy metals
-disulfide bonds aren’t broken at the temp which breaks hydrogen and ionic bonds

66
Q

What’s the test for proteins?

A

-add biuret reagent
-a purple, lilac or mauve colour= protein is present
-blue= no protein

67
Q

What type of proteins are enzymes?

A

-Tertiary, gobular proteins
-(gobular) so have a specific tertiary structure and a specific active site

68
Q

What are enzymes?

A

-biological catalysts
-regulating biological processes in living organisms

69
Q

What determines an enzymes specific function?

A

-the protein nature
-tertiary structure

70
Q

How do enzymes increase rate of reaction?

A

-lower activation energy (reaction can take place at lower temp)
-through formation of enzyme-substrate complexes
-by increasing rate of reaction the reaction happens quicker and more often

71
Q

What causes enzyme specificity?

A

-unique tertiary structure
-this structure is held together by: hydrogen, ionic bonds and sometimes disulfide bridges
-this determines the shape and electrostatic charge of the active site

72
Q

Explain the lock and key model.

A

-rigid
-the active site represents a small region of the enzyme molecule
-only substates with complementary shape to the active site will bind to it, forming an ENZYME-SUBSTRATE COMPLEX
-reaction takes place
-product is released from the active site
-enzyme remains unchanged at end of reaction

73
Q

What’s an enzyme-substrate complex?

A

-when an enzyme and substrate bind
-needed for reaction to start
-maybe more than one substrate binding to active site

74
Q

Explain the induced fit model.

A

-active site and enzyme can change shape slightly to become complementary
-the correct substrate can interact with active site
-enzyme is flexible and mould itself around the substrate

75
Q

How does the induced fit model help bonds form/break?

A

-puts strain on or distorts bonds which lowers activation energy to break bonds- easier to hydrolyse
-pushes two substrate together or causes two molecules to interact so its easier for bonds to form

76
Q

What are the factors that affect the rate of enzyme reactions?

A

-temperature
-concentration of enzyme
-pH
-substrate concentration
-inhibition

77
Q

What does increasing substrate concentration do with a given concentration of enzyme?

A

-increase rate of reaction to a particular point
-at which rate reaches a constant maximum rate
-where all active sites are SATURATED

78
Q

Describe and explain the effect of substrate conc on enzymic reactions.

A

-rate initially increases as successful collisions between enzyme and substrate molecules are more likely so more e-s complexes formed
-rate then plateaus as the active site of all the enzyme molecules are saturated
-rate of reaction is now limited by the time required for the e-s complexes to form the product and release it from the active site

79
Q

How do you increase rate of reaction at a higher substrate concentration?

A

Addition of more enzyme

Unit 1: Biological Molecules (1 decks)

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