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A-Level Biology > 1A - Biological Molecules > Flashcards

1A - Biological Molecules Flashcards

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1
Q

What are polymers?

A
  • large complex molecules

- long chains of monomers joined together

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2
Q

What are monomers?

A
  • small, basic molecular units
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3
Q

Name 3 examples of monomers

A
  • Monosaccharides
  • Amino acids
  • Nucleotides
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4
Q

What are Carbohydrates made from and what elements do they contain?

A
  • Monosaccharides

- Carbon (C), Hydrogen (H) and Oxygen (O)

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5
Q

Name 3 main monosaccharides

A
  • Glucose
  • Fructose
  • Galactose
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6
Q

What is glucose?

A
  • a hexose sugar (contains six carbon atoms)
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7
Q

Alpha and beta glucose are isomers. What are isomers?

A
  • molecules with the same molecular formula as each other but atoms are connected in different ways
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8
Q

What is a condensation reaction?

A
  • two molecules join together by a new chemical bond

- water molecule is released

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9
Q

What type of bond forms in condensation reaction?

A
  • Glycosidic
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10
Q

What is a disaccharide?

A
  • Two monosaccharides joined together
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11
Q

A glucose molecule and a fructose molecule join together to make what?

A
  • Sucrose
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12
Q

A glucose molecule and a galactose molecule join to make what?

A
  • Lactose
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13
Q

Two glucose molecules join to make what?

A
  • Maltose
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14
Q

What is a hydrolysis reaction?

A
  • where polymers are broken down into monomers

- water molecule is added and breaks the chemical bond

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15
Q

What are polysaccharides?

A
  • more than two monosaccharides joined together
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16
Q

Starch is a mixture which two polysaccharides?

A
  • Amylose

- Amylopectin

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17
Q

What is the structure of amylose?

A
  • long, unbranched chain of alpha glucose
  • coiled structure
  • compact (good for storage)
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18
Q

What is the structure of amylopectin?

A
  • long, branched chain of alpha glucose

- side branches allow enzymes to break down glycosidic bonds easily

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19
Q

What at the properties of starch?

A
  • insoluble in water (hydrophobic)
  • doesn’t affect water potential
  • they can swell up (good storage)
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20
Q

What do animals store excess glucose as?

A
  • Glycogen
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21
Q

What is the structure of glycogen?

A
  • similar to amylopectin but loads more side branches
  • side branches release glucose quickly
  • compact molecule
22
Q

Where would you find cellulose in a plant?

A
  • Cell wall
23
Q

What is the structure of cellulose?

A
  • long, unbranched chains of beta glucose
  • linked together by hydrogen bonds called microfibrils
  • microfibrils provide structural support
24
Q

What is the structure of a triglyceride?

A
  • one molecule of glycerol with 3 fatty acids attached to it
25
Q

How are triglycerides formed?

A
  • Condensation reactions
    (ester bonds form between three glycerol molecules)
  • water is released each time
26
Q

What do the terms hydrophobic and hydrophilic mean?

A
  • HydroPHOBIC means it’s insoluble in water

- HydroPHILIC means it’s soluble in water

27
Q

What is the difference between saturated and unsaturated fats?

A
  • Saturated fats do NOT have any double bonds between carbon atoms
  • Unsaturated fats have double bonds between carbon atoms
28
Q

What is the difference between the structures of triglycerides and phospholipids?

A
  • One of the fatty acid molecules in a triglyceride is replaced by a phosphate group
29
Q

What are the properties of triglycerides?

A
  • hydrocarbon tails contains a lot of chemical energy
  • insoluble (don’t affect water potential)
  • causes osmosis
30
Q

What are the properties of phospholipids?

A
  • make up bilayer of cell membranes
  • heads are hydrophilic and tails are hydrophobic - form double layer
  • water-soluble substances can’t easily pass through it
31
Q

What is a dipeptide?

A
  • Two amino acids joined together
32
Q

What is a polypeptide?

A
  • More than two amino acids joined together
33
Q

What are the different groups in the structure of amino acids?

A
  • Carboxyl group (COOH)
  • Amino group (H2N)
  • Variable/carbon containing group (R)
34
Q

In a condensation reaction, what type of bond is formed between two amino acids?

A
  • peptide bonds
35
Q

What is the primary structure of a protein?

A
  • sequence of amino acids in the polypeptide chain
36
Q

What is the secondary structure of a protein?

A
  • hydrogen bonds from between the amino acids

- coil into a helix or fold into a pleated sheet

37
Q

What is the tertiary structure of a protein?

A
  • coiled or folded further
  • more hydrogen and ionic bonds form
  • 3D structure
38
Q

What is the quaternary structure of a protein?

A
  • several different polypeptide chains held together by bonds
  • final 3D structure
39
Q

What are the 4 different functions of proteins?

A
  • Enzymes
  • Antibodies
  • Transport
  • Structural
40
Q

What are enzymes?

A
  • speed up chemical reactions acting as catalysts
  • spherical in shape
  • soluble
  • have roles in metabolism
41
Q

What are antibodies?

A
  • immune response

- two light polypeptide chains

42
Q

What are transport proteins?

A
  • contain hydrophobic and hydrophilic amino acids

- transport molecules and ions across membranes

43
Q

What are structural proteins?

A
  • physically strong

- long polypeptide chains lying parallel and form cross links

44
Q

How do enzymes lower the activation energy?

A
  • make reactions happen at lower temperatures

- speeding up the rate of reaction

45
Q

Why do scientists prefer the ‘induced fit’ model than the ‘lock and key’ model?

A
  • new studies showed the enzyme-substrate complex slightly changed shape to completely fit
46
Q

What are the properties of an enzyme?

A
  • very specific (only one complementary substrate can fit into an active site)
  • tertiary structure of the enzyme determines the active site’s shape
  • tertiary is determined by primary structure
  • primary structure is determined by a gene
47
Q

What are the 5 factors that can affect enzyme activity?

A
  • Temperature
  • pH
  • Enzyme concentration
  • Substrate concentration
  • Inhibitors (competitive and non-competitive)
48
Q

How does an enzyme become ‘denatured’?

A
  • active site changes shape

- enzyme and substrate can no longer fit together

49
Q

How does temperature affect enzyme activity?

A
  • more kinetic energy, so molecules faster
  • enzymes are more likely to collide
  • heavy vibrations causes bonds in enzyme to break if it’s too high
50
Q

What is the difference between competitive and non competitive inhibitors?

A
  • competitive bind to the active site

- non competitive bind to the enzyme away from active site, causing it to change shape

A-Level Biology (19 decks)

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