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‘Biological Molecules’ And ‘Cell Structure And Transport’ > Carbohydrates, Proteins, Lipids > Flashcards

Carbohydrates, Proteins, Lipids 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
Why are triglycerides ideal storage compounds?
- yield twice as much energy as carbohydrates when fully oxidised (respired) - insoluble so osmotically inactive
26
How are triglycerides formed?
-Joining 3 fatty acids to 1 glycerol molecule -during condensation reaction with the loss of 3 water molecules
27
What is the general formula of a fatty acid?
-R-COOH -R= long hydrocarbon chain -COOH= carboxylic acid group
28
Describe a saturated fatty acid.
-no double bonds between carbon atoms -straight chain -contains the most amount of hydrogen molecules it can -bad fats (eg. Butter)
29
Describe an unsaturated fatty acid.
-contain one or more double bonds between carbon atoms -kinky structure -kinks give it an oily texture -good fats (eg. Oils)
30
What’s the structure of glycerol?
31
What’s the bond formed between glycerol and a fatty acid in a condensation reaction?
Ester bond
32
How can lipids be hydrolysed?
-heating with acid or alkali -using lipase enzyme at an optimum temperature and pH
33
How can you test for lipids?
Emulsion test
34
Describe the emulsion test for lipids.
-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
What is a phospholipid?
A lipid containing a phosphate group. (Phospholipid replaces one of the fatty acid molecules)
36
What does a phospholipid consist of?
-1 glycerol -2 fatty acids -A phosphate group joined in a condensation reaction
37
Explain the structure of a phospholipid.
-has a phosphate polar hydrophilic head -two fatty acid non-polar hydrophobic tails
38
What happens when a thin layer of phospholipids are in contact with water?
-forms a single layer of -hydrophilic heads are attracted to the water -hydrophobic tails repel the water and project outwards
39
Where is a bilayer found?
Cell membrane
40
What’s a bilayer?
- two layers of phospholipids -hydrophobic tails are attracted to each other and repel the water
41
What’s the function of cholesterol in a bilayer?
-cholesterol inbetween phospholipids -increases stability of plasma -makes it less flexible
42
How does a bilayer effect permeability of the membrane?
- gives membrane selective permeability - select what they allow to go through the cell membrane
43
Why would red blood cells have a higher percentage of cholesterol than cell lining?
-red blood cells have no support so need lots of cholesterol -cells lining walls have supports and stability from the cells around them
44
What does protein contain?
-carbon -hydrogen -oxygen -nitrogen -sometimes sulphur
45
What’s the monomer of proteins?
Amino acids
46
What is the structure of an amino acid?
-amino group (NH2) -carboxylic acid group (COOH) -differ in the atomic group R
47
What is the bond between two animo acids?
A peptide bond (-CONH-) formed by condensation reactions
48
What do two animo acids joined together form?
Dipeptide
49
What does many animo acids joined together form?
Polypeptide
50
How can proteins be hydrolysed?
-heating with acid -using enzyme (protease) at its optimum temp
51
What’s the primary structure of a protein?
-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
What is the secondary structure of a protein?
-the PLEATING or COILING of the polypeptide chain -as a result of hydrogen bonding between amino acids -inc: helix, b-pleated sheet
53
What is the tertiary structure of a protein?
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
What does the tertiary structure of an enzyme determine?
The shape of its active site and its precise function
55
Draw a disulfide bridge
56
Draw a peptide bond
57
Draw an ester bond
58
Draw a glycosidic bond
59
What happens if you change the sequence of amino acids?
-causes mutations -could change shape of active site -causing enzyme to be non-functional or have a different function
60
What are Gobular proteins?
-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
What are fibrous proteins?
-typically long, thin and insoluble -have structural functions eg. Keratin in hair, collagen in connective tissues
62
What’s the quaternary structure?
highly complex proteins consisting of more than one polypeptide chain. Eg. Adult haemoglobin consists of four polypeptide chains
63
What bonds hold together a quaternary structure?
-ionic -hydrogen -disulfide bridges -hydrophobic interactions
64
What’s the denaturation of proteins?
-alteration in the tertiary structure of a protein -loss of 3D shape is often irreversible and protein is no longer functional
65
What causes the denaturation of proteins?
-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
What’s the test for proteins?
-add biuret reagent -a purple, lilac or mauve colour= protein is present -blue= no protein
67
What type of proteins are enzymes?
-Tertiary, gobular proteins -(gobular) so have a specific tertiary structure and a specific active site
68
What are enzymes?
-biological catalysts -regulating biological processes in living organisms
69
What determines an enzymes specific function?
-the protein nature -tertiary structure
70
How do enzymes increase rate of reaction?
-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
What causes enzyme specificity?
-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
Explain the lock and key model.
-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
What’s an enzyme-substrate complex?
-when an enzyme and substrate bind -needed for reaction to start -maybe more than one substrate binding to active site
74
Explain the induced fit model.
-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
How does the induced fit model help bonds form/break?
-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
What are the factors that affect the rate of enzyme reactions?
-temperature -concentration of enzyme -pH -substrate concentration -inhibition
77
What does increasing substrate concentration do with a given concentration of enzyme?
-increase rate of reaction to a particular point -at which rate reaches a constant maximum rate -where all active sites are SATURATED
78
Describe and explain the effect of substrate conc on enzymic reactions.
-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
How do you increase rate of reaction at a higher substrate concentration?
Addition of more enzyme

‘Biological Molecules’ And ‘Cell Structure And Transport’ (7 decks)

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