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Biological molecule Flashcards

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Biology 101 flashcards
1
Q

What is a monomer?

A

Smaller units which can create larger molecules

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2
Q

What is a polymer?

A

A chain of monomers bonded together

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3
Q

Examples of monomers and their polymers

A
  • Glucose: Starch, Cellulose, Glycogen
  • Amino acid: Protein
  • Nucleotide: DNA + RNA
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4
Q

Monomer for carbohydrates and examples

A

Monosaccharides:
- Fructose
- Glucose
- Galactose

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5
Q

Structure of a-glucose

A
  • C6H12O6
  • H-OH on carbon 1 + 4
  • O before carbon 1
  • Methyl group on carbon 5
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6
Q

Structure of B-glucose

A
  • C6H12O6
  • OH-H on carbon 1
  • H-OH on carbon 4
  • O before carbon 1
  • Methyl group on carbon 5
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7
Q

Describe disaccharides and examples

A
  • 2 monosaccharides joined by a glycosidic bond
  • Formed via condensation reaction
    EXAMPLES:
  • glucose+glucose = maltose
  • glucose+galactose = lactose
  • glucose+fructose = sucrose
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8
Q

Describe condensation reaction

A

Joining of 2 molecules together by removing water

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9
Q

Describe hydrolysis reaction

A

Splitting apart molecules by the addition of water

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10
Q

Describe polysaccharides and examples

A

Condensation reaction between many glucose monomers
EXAMPLES:
- Starch
- Cellulose
- Glycogen

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11
Q

Describe starch

A
  • Alpha-glucose
  • Store of glucose in plant cells
  • Insoluble so doesn’t affect WP
    AMYLOSE:
  • 1-4 glycosidic bond
  • Unbranched helix
  • Helix = compact so can fit a lot of glucose into small spaces
    AMYLOPECTIN:
  • 1-4/1-6 glycosidic bond
  • Branched molecule
  • Branched = increased SA for rapid hydrolysis back to glucose
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12
Q

Describe glycogen

A
  • Alpha-glucose
  • 1-4/1-6 glycosidic bonds
  • Store of glucose in animal cells e.g. muscle + liver cells
  • Highly branched structure
  • Branched = increased SA for rapid hydrolysis back to glucose
  • Insoluble = won’t affect WP
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13
Q

Describe cellulose

A
  • Beta-glucose
  • 1-4 glycosidic bonds
  • Provides structural support + strength to plant cell wall
  • polymer forms long straight chains held parallel to each other with H-bonds = fibrils
  • H-bonds = Collective strength so avoid bursting under pressure
  • Insoluble = won’t affect WP
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14
Q

Describe how triglycerides are formed

A
  • Condensation reaction 1 glycerol molecule + 3 fatty acids
  • Forms 3 ester bonds + 3 water molecules
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15
Q

Describe a saturated fatty acid

A

The hydrocarbon chain has only single bonds between carbons

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16
Q

Describe a unsaturated fatty acid

A

The hydrocarbon chain has at least 1 double bond between carbons

17
Q

Properties of triglycerides

A

1) High enerygy:mass = C-H bonds store a lot of energy
2) Metabolic water source = Can release water when oxidized which is beneficial for desert animals
3) Insoluble = Don’t affect WP as the hydrocarbon chain is hydrophobic
4) Slow heat conduction = Good for thermal insulation
5) Less dense than water = Buoyancy in aquatic animals

18
Q

Structure of phospholipid

A
  • Phosphate attached to glycerol = Hydrophilic head
  • 2 fatty acid chains attached to glycerol = Hydrophobic tail
  • 2 fatty acid bond via 2 condensation reactions = 2 ester bonds
19
Q

Properties of phospholipids

A
  • 2 different charged regions = polar
  • Can form the phospholipid bilayer with the hydrophilic heads on the outside and hydrophobic tails on the inside = cell membrane
  • Hydrophobic tails can splay outwards = waterproofing
20
Q

Structure of an amino acid

A

. R
I
NH2 – C – COOH
I
H
- NH2 = Amine group
- COOH = Carboxyl group
- R = Variable group of 20 options

21
Q

Describe how a dipeptide is formed

A
  • Condensation reaction between the OH of carboxyl group and H of amine group of another
  • H2O removed = Peptide bond
22
Q

Describe primary structure

A

The sequence of amino acids in the polypeptide chain = polymer

23
Q

Importance of primary structure

A
  • A difference in even 1 amino acid in the sequence = bonds will form in different locations = different 3’ + 3D structure
  • e.g. enzyme + carrier proteins
24
Q

Describe secondary structure

A
  • The specific sequence causes protein molecule to bend into a-helix or fold into B-pleated sheet
  • H-bonds form between C=O in carboxyl group of 1 amino acid and H in the amine group of another
25
Q

Describe tertiary structure

A
  • Further folding for 2’ structure
  • Forms unique 3D shape
  • Held in place by H-bond/ionic/disulfide bonds
  • H-bonds = Between C=O + H
  • Ionic bond = Between R groups of opposing charges
  • Disulphide bonds = Between S-S between R groups
26
Q

Describe quaternary structure

A

More than 1 polypeptide chain bonded by H-bonds/ionic/disulfide bonds

27
Q

Describe denaturing of proteins

A
  • Bonds which hold the 2’/3’ break = 3’ 3D structure is lost
  • Caused by increased heat = too much KE
  • Caused by increase/decreased pH = too many OH-/H+
28
Q

Biochemical test for starch

A
  • Add iodine to sample
  • Positive = blue/black
29
Q

Biochemical test for reducing sugar

A
  • Add benedict’s reagent + heat
  • Positive test = green-yellow-orange-brick red
  • The higher the concentration = more red
30
Q

Biochemical test for non-reducing sugar

A
  • Negative benedict’s = stays blue
  • Add HCl + boil
  • Cool sample then add sodium carbonate = neutralize = broken glycosidic bonds
  • Add benedict’s reagent + heat
  • Positive test = green-yellow-orange-brick red
31
Q

Biochemical test for proteins

A
  • Add biuret to sample
  • Positive test = from blue to purple
32
Q

Biochemical test for lipids

A
  • Dissolve in ethanol
  • Add distilled water
  • Positive test = white emulsion
33
Q

Describe an enzyme

A
  • Tertiary structure proteins = catalyze reactions
  • When attached with substrate = lower AE needed for reaction to occur = speeds up
34
Q

Describe the active site

A
  • Where the substrate attaches to the enzyme
  • Specific shape = folding/bonding in 3’
  • Specificity = only complementary substrate can bind
35
Q

Describe the lock and key model

A
  • Enzyme = lock / Substrate = key
  • Enzyme active site is a rigid + fixed shape
  • Enzyme-substrate complexes form due to random collisions
  • This puts strains on the substrate bonds = lowered activation energy
36
Q

Describe the induced fit model

A
  • Shape of active site is not initially complementary but flexible
  • The active site is induced and shape changes to model around the substrate
  • Moulding = strain on bonds = lower AE
37
Q

How does temperature affect enzymes

A

TOO LOW:
- Not enough KE for successful collisions between enzyme + substrate
TOO HIGH:
- Enzyme denatures = active site shape changes = can’t form enzyme-substrate complex

38
Q

How does pH affect enzymes

A
  • Enzyme denatures = fewer enzyme-substrate complexes form
  • Enzymes must be optimum pH
    TOO HIGH:
  • Too many OH- interfere with charges on aminos in active site = breaks bonds holding 3’ = shape changes
    TOO LOW:
  • Too many H+ interfere with charges on aminos in active site = breaks bonds holding 3’ = shape changes
39
Q

How does concentrations affect enzymes

A

INSUFFICIENT SUBSTRATE:
- Reaction will be slower as there will be collisions = empty active sights = line plateau
INSUFFICIENT ENZYME:
- Active sites will become saturated with substrate = unable to work faster as all active sites are in use = line plateau

BIO (20 decks)

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