1.1 (1) - Biological Molecules Flashcards

Introduction to biological molecules Carbohydrates and monosaccharides Carbohydrates - disaccharides and polysaccharides Starch, glycogen and cellulose Lipids Proteins Enzyme action Enzyme inhibition

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1
Q

What is a monomer?

A

1 single unit of a polymer

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2
Q

What is a polymer?

A

A chain of monomers, making a larger molecule

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3
Q

What is the function of carbohydrates?

A
  • Commonly used as respiratory substrates

- Structural components in plasma membranes and cell walls

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4
Q

What is the function of lipids?

A
  • Insulation
  • Energy source
  • Help create cell membranes
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5
Q

What is the function of proteins?

A

Form many cell structures

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6
Q

What is the function of nucleic acid?

A

Used for production to make genetic material

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7
Q

What is a respiratory substrate?

A

A molecule that can release energy to produce ATP in a cell

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8
Q

What kind of sugar is a monosaccharide?

A

Hexose sugar

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9
Q

What is the difference between an ɑ-glucose and a β-glucose?

A

ɑ-glucoses have their hydroxyl below Carbon 1

β-glucoses have their hydroxyl above Carbon 1

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10
Q

What kind of reaction are monosaccharides formed during?

A

Condensation reaction

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11
Q

What bond are 2 monosaccharides joined together in a disaccharide by?

A

Glycosidic bond (covalent)

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12
Q

What is a carbohydrate monomer called?

A

Monosaccharide

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13
Q

What are the 3 main monosaccharides?

A
  • Glucose
  • Fructose
  • Galactose
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14
Q

What are 2 monosaccharides joined together called?

A

Disaccharides

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15
Q

What are the 3 main disaccharides?

A
  • Maltose
  • Sucrose
  • Lactose
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16
Q

What 2 monosaccharides make up maltose?

A

2 ɑ-glucoses

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17
Q

What 2 monosaccharides make up sucrose?

A

1 glucose and 1 fructose

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18
Q

What 2 monosaccharides make up lactose?

A

1 glucose and 1 galactose

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19
Q

What are many monosaccharides joined together called?

A

Polysaccharides

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20
Q

What are the 3 main polysaccharides?

A
  • Cellulose
  • Glycogen
  • Starch
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21
Q

What monosaccharides is cellulose made up of?

A

Chains of β-glucoses

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22
Q

What monosaccharides is glycogen made up of?

A

Chains of ɑ-glucoses

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23
Q

What monosaccharides is starch made up of?

A

Chains of ɑ-glucoses

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24
Q

What is a condensation reaction?

A

When two monosaccharides join and a water molecule is removed

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25
Q

What is a hydrolysis reaction?

A

When water is added to a disaccharide to break the glycosidic bond between the 2 monosaccharides

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26
Q

What is a reducing sugar?

A

One that can donate electrons to another chemical

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27
Q

Describe the Benedict’s Test

A

1) Add 2cm3 of food sample to a test tube in a paste / liquid form
2) Add 2cm3 of Benedict’s reagent
3) Heat the mixture gently over a water bath for 5 minutes

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28
Q

What are the test results (colours) for the Benedict’s Test?

A
Blue - None present
Green - Trace
Yellow - Low
Orange/red - Moderate
Maroon - High
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29
Q

Is the Benedict’s Test quantitative or semi-quantitative?

A

Semi-quantitative

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30
Q

What is a semi-quantitative test?

A

It doesn’t measure the precise quantity of a substance, BUT the result expresses an estimate of how much of a detected substance is present (eg. colour spectrum)

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31
Q

What is the test for non-reducing sugars?

A

1) Make sure the food sample is liquid
2) Add 2cm3 of food sample to 2cm3 of Benedict’s reagent in a test tube → filter
3) Place test tube in water bath for 5 minutes. If the colour does NOT change, reducing sugars are NOT present
4) In a new test tube, add 2cm3 of food sample to 2cm3 dilute hydrochloric acid (DHA) and put into a water bath for 5 minutes. The DHA will hydrolyse any NON-REDUCING disaccharides present into its REDUCING monosaccharides
5) Slowly add some sodium hydrogen carbonate solution to the test tube (neutralising it). Test with pH paper, the solution should be alkaline
6) Re-test the resulting solution by heating it with 2cm3 Benedict’s reagent in a water bath for 5 minutes
7) If a non-reducing sugar was present in the original sample, the reagent will now turn brown-orange, because of the reducing sugars that were produced from the hydrolysis of the non-reducing sugars

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32
Q

Describe starch

A
  • Plant energy-storage molecule
  • It makes it insoluble, so that they don’t draw water into the cell and affect water potential
  • Doesn’t dissolve, so there is no effect on osmotic potential, it won’t diffuse
  • It can be hydrolysed to ɑ-glucoses, which is easy to transport and good for respiration
  • It can take a more-branched structure which has more ends, speeds up its break down
  • Forms close spiral structures - allows it to be tightly packed
33
Q

Describe glycogen

A
  • Found in animals
  • Insoluble
  • Function - energy storage and release molecule
  • Forms a many-branched structure, so that there are lots of ends for glucose to be released from
34
Q

Describe cellulose

A
  • Structural carbohydrate
  • β-glucoses are ALTERNATING (flipped over), forming really strong chains
  • Dietary fibre
35
Q

What three chemical elements are lipids composed of?

A

Carbon (C), hydrogen (H) and oxygen (O)

36
Q

Do lipids have a lower or higher proportion of oxygen to carbon and hydrogen than carbohydrates?

A

Lower proportion

37
Q

What substances are lipids soluble / insoluble in?

A

Soluble - organic substances (eg. alcohol and acetone)

Insoluble - water

38
Q

What are 4 functions of lipids?

A
  • Energy storage molecule
  • Waterproofing
  • Insulation
  • Physical protection
39
Q

If it is solid between 10°C and 20°C, the lipid is a…

A

Fat

40
Q

If it is liquid between 10°C and 20°C, the lipid is an…

A

Oil

41
Q

What is the structure of a triglyceride?

A

3 fatty acids with a glycerol molecule joined via an ester bond

42
Q

What is the main cause of fatty acid variation?

A

Saturation

43
Q

How many double bonds does a monounsaturated fatty acid have?

A

1 double bond

44
Q

How many double bonds does a saturated fatty acid have?

A

0 double bonds

45
Q

How many double bonds does a polyunsaturated fatty acid have?

A

More than 1 double bond

46
Q

How is a phospholipid different to a triglyceride?

A

One of the fatty acids is replace with a hydrophilic phosphate molecule

47
Q

What do phospholipid bilayers help to make?

A

Cell membrane

48
Q

What is the significance of phospholipids being polar?

A

They can form bilayers in aqueous solutions, forming a barrier between the intercellular and extracellular fluid

49
Q

Phospholipid structure aids with the formation of…

A

Glycolipids

50
Q

Describe the emulsion test for lipids

A

1) Take a clean, dry test tube
2) Add 5cm3 ethanol to 2cm3 of food sample
3) Shake the tube thoroughly to dissolve any lipid in the sample
4) Add 5cm3 water, shake gently
5) A cloudy-white emulsion indicates the presence of a lipid
6) As a control, repeat the procedure using water instead of the food sample; the control should remain clear

51
Q

What are the monomers of proteins called?

A

Amino acids

52
Q

What is the generic structure of a protein?

A
  • Central ɑ-carbon
  • Amino group (left - H-N-H)
  • Solitary hydrogen (above)
  • Carboxyl group (right - OH-C=O)
  • R-group (varies the protein)
53
Q

How many types of amino acids are proteins made of?

A

All 20 amino acids

54
Q

What is the name of a polymer of amino acids joining together?

A

Polypeptide

55
Q

What is the joining of many monomers to make a polymer called?

A

Polymerisation

56
Q

What bond are amino acids joined by?

A

Peptide bond

57
Q

What molecule is formed between the -OH from the carboxyl group when 2 amino acids join?

A

Water molecule

58
Q

Describe a protein’s primary structure

A
  • A chain of amino acids
  • It is determined by the type, sequence and number of amino acids
  • It determines the shape, structure and function of the protein because of the r-group and different molecular structure
59
Q

Describe a protein’s secondary structure

A
  • Occurs as H bonds form between the +charged H of the -NH and the -charged oxygen of the -C=O group
  • The H bonds tend to be weak, but they are strong enough to twist the polypeptide chain into a 3D shape (ɑ helix OR β-pleated sheet)
60
Q

Describe a protein’s teritary structure

A
  • It is determined by the primary structure
  • It’s the result of further twisting of the secondary structure
  • Plays a significant role in determining the protein’s behaviour
  • Maintained by:
    • Disulfide bonds
    • Hydrogen bonds
    • Ionic bonds
61
Q

Describe a protein’s quaternary structure

A
  • Consists of 2 or more polypeptide chains bonded together
  • Some large proteins also include a non-peptide part, called a prosthetic group (eg. inorganic iron ions are the prosthetic group in haemoglobin)
62
Q

What 5 factors affect the rate of enzyme-controlled reactions?

A
  • Enzyme concentration
  • Substrate concentration
  • Concentration of competitive and non-competitive inhibitors
  • Temperature
  • pH
63
Q

What 3 things are needed for chemical reactions to occur naturally?

A
  • Reactants must collide with enough energy to change their atom arrangement
  • The free energy of the products must be less than that of the reactants (substrates)
  • There must be enough activation energy
64
Q

What kind of protein is an enzyme?

A

Globular protein

65
Q

What is the shape of an enzyme’s active site detemined by?

A

The protein’s tertiary structure

66
Q

What is a protein’s primary structure determined by?

A
  • Which amino acids are present
  • How many are present
  • What order they’re arranged in
67
Q

In the Induced Fit Model (IFM), how to enzymes, substrates and active sites fit together?

A
  • The active site of an enzyme only takes the shape of the substrate when they collide
  • The flexibility of the polypeptide chains in the enzyme allows it to change the shape of its active site around the substrate, if all the right bonds can be formed in all the right places
  • If this happens, the reaction can happen
68
Q

How is the enzyme able to shape its active site around a substrate?

A

The flexibility of the polypeptide chains allows the active site to shape the substrate, only if all the right bonds can be formed in all the right places

69
Q

What is the molecule called that forms between an enzyme and a substrate when they bond?

A

Enzyme-substrate complex

70
Q

How does temperature affect the rate of enzyme-catalysed reactions?

A

If the temperature is increased, the active site starts to denature, so the enzyme can’t fit withe the substrate, so it can’t catalyse the reaction

71
Q

How does pH affect the rate of enzyme-catalysed reactions?

A
  • The hydrogen and ionic bonds (in the enzyme) will be disrupted by the presence of H+ or OH- ions
  • If the ionic bonds are swamped with H+ or OH- ions, the electrostatic forces of attraction will be interfered with and they’ll weaken
  • Changes in pH away from the enzyme’s optimum pH will interfere with the hydrogen and ionic bonds in the enzyme’s tertiary structure
  • The shape changes and the active site no longer matches the substrate, so the enzyme can’t react with it
72
Q

What does a higher concentration of substrates mean for the reaction?

A

Means that it’s more likely for a substrate to bind with an active site

73
Q

What does ‘inhibition’ mean?

A

Certain “inhibitor molecules” can prevent an enzyme from working

74
Q

What are the 2 types of enzyme inhibition?

A
  • Competitive inhibition

- Non-competitive inhibition

75
Q

Describe competitive inhibition

A

When a molecule, other than an enzyme-specific substrate, is complementary to the active site of the enzyme and stops the reaction from being catalysed

76
Q

Describe non-competitive inhibition

A
  • Doesn’t occupy the active site
  • They attack the allosteric site, distorting the shape of the active site so that it’s not longer complementary to the substrate
77
Q

Describe how inhibitors affect enzymes

A
  • Competitive inhibitor mimics substrate and competes for the active site
  • Non-competitive inhibitor alters conformation of enzyme so active site is no longer fully functioning
78
Q

Which type of lipid is a good energy-storage molecule? Why?

A

Triglyceride - there is a higher ratio of carbon-hydrogen bonds to oxygen bonds