Biological molecules Flashcards

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1
Q

What are biological molecules

A

molecules made and used by organisms

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2
Q

Functions of carbohydrates

A
  • energy source (glucose in respiration
  • energy store (starch in plants, glycogen in animals)
  • structure (cellulose in cell wall of plants)
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3
Q

What are the building blocks for carbohydrates

A

monosaccharides

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4
Q

Name the three monosaccharides

A
  • glucose
  • galactose
  • fructose
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5
Q

Difference between a and b glucose

A

on carbon 1, OH on bottom for a- glucose, on top for b- glucose

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6
Q

How are monosaccharides joined together

A

condensation reaction (removing water), between 2 OH groups

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7
Q

Bond in a carbohydrate

A

1,4 glycosidic bond

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8
Q

Name the disaccharides

A
  • Maltose (glucose + glucose)
  • Lactose (glucose + galactose)
  • Sucrose (glucose + fructose)
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9
Q

How are polymers separated

A

hydrolysis reaction (add water)

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10
Q

What is a polysaccharide

A

many monosaccharides joined together by condensation reaction, forming glycosidic bonds

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11
Q

Name the polysaccharides

A
  • Starch (long chain of alpha glucose)
  • Glycogen (long chain of alpha glucose
  • Cellulose (long chain of beta glucose)
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12
Q

Function of each polysaccharide

A
  • Starch, energy store in plants
  • Glycogen, energy store in animals
  • Cellulose, makes up cell wall in plants
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13
Q

Polysaccharides summary

A
  • carbohydrates made up of long chain of monosaccharides joined by condensation reaction, forming glycosidc bonds
  • 3 examples: starch, glycogen, cellulose
  • Starch + Glycogen used as energy store (starch for plants, glycogen for animals) as they’re made of many a-glucose which are used for respiration
  • Cellulose used to form cell wall of plants, made of many b-glucose
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14
Q

Structure of starch

A
  • made of amylose (1,4 glycosidic bonds) + amylopectin (1,4 + 1,6 glycosidic bonds)
  • long unbranched chain of coiled a-glucose (amylose)
  • long chain of a-glucose with side branches (amylopectin)
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15
Q

Structure of glycogen

A

straight chain of a-glucose 1,4 glycosidic bonds with side branches (1,6 glycosidic bonds)

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16
Q

Properties of starch and glycogen

A
  • insoluble (don’t affect water potential, don’t diffuse out of cell)
  • coiled/branched, more can fit into cell
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17
Q

Structure of cellulose

A
  • b-glucose arranged in a straight chain
  • hydrogen bonds present to form microfibrils
  • many microfibrils are cross linked to form macrofibrils
  • this forms structure of cell wall
  • strong material prevents cell from bursting
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18
Q

Test for starch

A

add iodine, turns blue/black

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19
Q

Test for reducing sugar

A

heat with benedicts, turns brick red

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20
Q

Test for non-reducing sugar

A
  • heat with benedicts, no change
  • add dilute hydrochloric acid
  • add sodium hydrogencarbonate to neutralise solution
  • heat with benedicts, turns brick red
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21
Q

What are fibrous proteins

A

strong, insoluble, inflexible material; like collagen

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22
Q

What are the building blocks for proteins

A

amino acids

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23
Q

Structure of an amino acid

A
  • central carbon
  • carboxyl group to the right (COOH)
  • amine group to the left (NH2)
  • hydrogen above, R group below
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24
Q

How do amino acids differ

A

different R groups

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25
Q

How are amino acids joined together

A

by condensation reaction between carboxyl group of one and amine group of another, forming peptide bonds

26
Q

Describe primary, secondary, tertiary and quaternary structures

A
  • Primary, sequence of amino acids in a polypeptide chain held by peptide bonds
  • Secondary, polypeptide chain coils to form alpha helix + beta pleated sheets held by hydrogen bonds
  • Tertiary, secondary structure folds again to form 3D shape held by hydrogen, ionic and disulfide bonds
  • Quaternary, made up of two or more polypeptide chains
27
Q

Test for protein

A

add biuret solution, turns purple

28
Q

What is an enzyme

A

a biological catalyst which speeds up rate of reaction without being used up by lowering activation energy

29
Q

What makes an enzyme specific

A
  • has specific active site shape
  • only complementary substrates can bind to active sites to form ES complexes
30
Q

Describe the lock and key model

A

active site shape is rigid, only complemntary substrates can bind to form ES complexes

31
Q

Describe the induced fit model

A

active site changes shape, substrate binds to active site; changes shape so substrate becomes complementary, forming ES complex

32
Q

Effect of substrate concentration on enzyme activity

A
  • increasing substrate concentration increases chance of successful collisions, increasing chance of forming ES complexes, increases rate of reaction
  • continues until all substrates are used up
33
Q

Effect of temperature on enzyme activity

A
  • temp increase =
  • kinetic energy increases
  • molecules move faster, increasing chance of successful collisions, increasing number of ES complexes formed, increasing rate of reaction
34
Q

Overly high temperatures vs enzyme activity

A
  • bonds in tertiary structure break
  • active site changes shape so substrate no longer complementary
  • can’t form ES complexes so enzyme denatures
35
Q

Effect of pH on enzyme activity

A

if pH is changed from optimum, bonds in tertiary structure break, active site changes shape so no longer complementary to substrate, can’t form ES complexes, enzyme denatures

36
Q

Role of a competitive inhibitor

A

substance with similar shape to substrate binds to active site, blocking it, preventing ES complexes from forming

37
Q

Role of a non-competitive inhibitor

A

substance binds to allosteric site of enzyme, causes active site to change shape, so less ES complexes form

38
Q

3 types of lipids

A
  • triglycerides
  • phospholipids
  • cholesterol
39
Q

Role of each lipid

A
  • triglycerides, fat for energy store, insulation, protection of organs
  • phospholipids, to make membranes
  • cholesterol, for membrane stability and make hormones
40
Q

Structure of triglycerides

A
  • made of 1 glycerol and 3 fatty acids
  • joined by condensation reactions, forming ester bonds
41
Q

Saturated vs unsaturated chains

A

unsaturated contain C=C bonds, saturated do not

42
Q

Structure of phospholipids

A
  • made of 1 glycerol, 2 fatty acids and a phosphate group
  • phosphate forms hydrophilic head (water loving), fatty acids form hydrophobic tails (water hating)
  • forms phospholipid bilayer
43
Q

What are nucleic acids

A

polymers made from nucleotides (2 types, DNA and RNA)

44
Q

What is DNA

A
  • deoxyribonucleic acid
  • found in all organisms
  • carries genes
45
Q

What is a gene

A

section of DNA that codes for a protein

46
Q

Building block of DNA

A
  • DNA nucleotide, made up of phosphate, deoxyribose sugar and nitrogenous base
47
Q

Name the 4 types of nucleotide

A
  • adenine
  • thymine
  • cytosine
  • guanine
48
Q

Describe the structure of DNA

A
  • consists of polynucleotides
  • each nucleotide formed from deoxyribose, phosphate group and nitrogenous base
  • phosphodiester bonds between nucleotides
  • double helix held by hydrogen bonds
  • hydrogen bonds occur between adenine, thymine and cytosine, guanine
49
Q

Describe the process of semi-conservative DNA replication

A
  • DNA helicase breaks hydrogen bonds between the complementary bases
  • double strand separates, leaving two template strands
  • free DNA nucleotides bind to exposed complementary base pairs
  • DNA polymerase catalyses the condensation reaction which joins the nucleotides together
  • each new DNA molecule contains one strand of original and one strand of new DNA
50
Q

What is RNA made up of

A
  • ribose sugar
  • phosphate group
  • nitrogenous base (AUCG)
51
Q

2 types of RNA

A
  • mRNA (messenger RNA)
  • tRNA (transfer RNA)
52
Q

Similarities between mRNA and tRNA

A
  • both single stranded
  • both made of RNA nucleotides
53
Q

What is ATP

A

adenosine triphosphate, delivers energy for life processes

54
Q

Structure of ATP

A
  • ribose
  • adenine
  • 3 phosphate groups
55
Q

Describe the formation of ATP

A
  • ADP + Pi + energy used = ATP
  • occurs via a condensation reaction using ATP synthase
  • carries energy in its bonds
56
Q

Describe the breakdown of ATP

A
  • ATP= ADP + Pi + energy released
  • occurs via hydrolysis reaction using ATP hydrolase
  • releases energy from its bonds
57
Q

What makes ATP a good energy deliverer

A
  • immediate source, only need to break one weak bond
  • manageable source, releases small amounts of energy
58
Q

3 Uses of ATP in organisms

A
  • protein synthesis
  • metabolic reactions
  • active transport
59
Q

Properties of water

A
  • dipolar, positively charged hydrogen, negatively charged oxygen, so H2O molecules can form hydrogen bonds with each other
60
Q

Role of water in living organisms

A
  • a solvent so allowing transport of substances
  • high specific heat capacity so resists changes in temperature
  • a metabolite in photosynthesis
  • cohesion between water molecules so supports columns of water
  • large latent heat of vaporisation so provides cooling effect
61
Q

What are inorganic ions

A

salts/minerals that don’t contain carbon and are charged