3.1 Biological Molecules

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265 Terms

1

What is a nucleic acid

Polymers of nucleotides which contain genetic information

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2

How is DNA protected from mutations

By forming a double strand

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3

What base pairs does DNA contain

Cytosine, Thymine, Guanine, Adenine

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4

What is the function of mRNA

To transport information from nucleus to ribosomes

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5

What is the function of tRNA

To bring the amino acid to a ribosome

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6

What is the function of rRNA

To form part of the ribosome structure with proteins

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7

What bases make up RNA

Adenine, Uracil, Guanine, Cytosine

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8

What is the full name of DNA

Deoxyribonucleic acid

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9

What is the full name of RNA

Ribonucleic acid

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10

What is the general function of DNA and RNA

To build proteins and carry information

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11

What is the function of DNA

To hold or store genetic information

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12

What is the function of RNA

To transfer the genetic code from the nucleus to the ribosomes

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13

What molecules make up a nucleotide

A pentose sugar, a nitrogen containing base and a phosphate group

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14

Define nucleotides

Repeating monomers of DNA and RNA

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15

What is the difference between an RNA and DNA sugar

DNA contains deoxyribose sugar with H and the second position, RNA contains ribose sugar with OH in the second position

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16

What is the difference between DNA and RNA bases

RNA contains a uracil base instead of a thymine

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17

Define and give examples of purines

A nitrogenous base molecules with a double ring structure, such as adenine and guanine

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18

Define and give examples of pyrimidines

A nitrogenous base molecule with a single ring structure, such as cytosine, thymine and uracil

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19

Describe a difference between the structure of DNA and RNA

DNA is double stranded in a double helix, RNA is relatively short single strands

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20

What bond forms between nucleotides

A condensation reaction forms a phosphodiester bond

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21

How can the double helix strands be described

As antiparallel strands

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22

Describe the joining of two bases

Complementary base pairings are joined with hydrogen bonds

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23

How many bonds does thymine and adenine have

2 hydrogen bonds

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24

How many bonds does cytosine and guanine have

3 hydrogen bonds

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25

Describe an RNA polymer

A relatively short, singular polynucleotide strand

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26

Name the types of RNA

messenger RNA, transfer RNA and ribosomal RNA

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27

Define a ribosome

A small organelle which are the site of protein synthesis and translation

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28

Where are ribosomes found

Either free in the cytoplasm or attached to the rough endoplasmic reticulum

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29

Describe the difference between prokaryotic and eukaryotic ribosomes

Eukaryotic ribosomes are 80s (60&40 subunits), prokaryotic ribosomes are 70s (30&50 subunits)

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30

Describe the structure of a ribosome

A small and large subunit, where the large unit is the sight of translation

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31

Who discovered DNA

Friedrich Miescher in 1800s

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32

Who discovered the double helix structure of DNA

Watson and Crick in 1953

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33

Describe why DNA nucleotides are added in the 5’ to 3’ direction

DNA polymerase is specific and the 5’ and 3’ ends of nucleotides are different shapes and therefore can only be complementary with the 3’ end of a developing strand

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34

Describe how the structure of RNA differs from DNA

RNA is single stranded, contains ribose sugar, uracil instead of thymine

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35

Suggest how changing the sequence of DNA nucleotides can affect the final product the DNA codes for

Different sequence of amino acids produces a different tertiary structure so the protein can no longer function

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36

Describe why nucleotides can only be added in a 5’ to 3’ direction

DNA polymerase is specific and the 5’ and 3’ ends of nucleotides are different shapes and therefore can only be complementary with the 3’ end of a developing strand

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37

How can drugs prevent DNA replication

By preventing complementary base pairing

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38

What is the purpose of DNA replication

To copy the DNA so two new daughter cells can be produced with full copies of parental DNA

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39

Describe semi-conservative replication

The process where one of the polynucleotide strands from the original DNA is used as a template

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40

Why is semi-conservative replication important

To ensure genetic continuity, replacement and growth of cells

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41

Describe the role of DNA helicase in semi-conservative replication

Breaking hydrogen bonds between base pairs, to unwind the DNA

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42

Describe the role of DNA polymerase in semi-conservative replication

Catalyses condensation reactions to form a new strand

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43

Describe semi-conservative replication

DNA helicase unwinds DNA, original polynucleotide acts as a template for free nucleotides, new nucleotides are joined by DNA polymerase

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44

Who discovered semi-conservative replication

Meselson and Stahl

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45

How did Meselson and Stahl discover semi-conservative replication

With 14N and 15N nitrogen

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46

Why is semi-conservative replication important

To ensure genetic information is passed from one generation to the rest

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47

How did Nitrogen show DNA replication

Combined densities in a N14 and N15 combination

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48

What is a polynucleotide

Half of a double helix strand

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49

What starts the semi-conservative replication process

Unwinding of the double helix

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50

What bonds does DNA polymerase form

Phosphodiester bonds

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51

What structure are enzymes

Globular

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52

What is enzymes effects on rate of reaction

Speeds the up as they are biological catalysts

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53

How do enzymes act as biological catalysts

By reducing activation energy without being used up or changed

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54

What is the active site on an enzyme specific to

A specific substrate

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55

Define intracellular enzymes

Produced and functioning inside the cell

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56

Define extracellular enzymes

Secreted by cells and catalyse reactions outside the cells

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57

What do enzymes and substrates react with

Induced fit

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58

How does the induced fit theory work

Substrate reacts with amino acids around the active site changing the tertiary structure to allow substrate to fit

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59

Describe catabolic reactions

Breakdown of complex molecules into simpler products

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60

Give examples of catabolic reactions

Cellular respiration and hydrolysis

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61

Define anabolic reactions

Reactions involving building a more complex molecule from simpler ones

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62

Give examples of anabolic reactions

Protein synthesis and photosynthesis

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63

What happens when temperature of enzymes increases

Kinetic energy increases meaning more successful collisions so more enzyme substrate complexes form

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64

Define denaturing

Ionic and hydrogen bonds break which changes the tertiary structure of the active site so is no longer complementary to the substrate

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65

Name all limiting factors affecting enzymes

Temperature, pH and enzyme concentration

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66

What happens when the enzyme goes above optimum temperature

It denatures

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67

What happens to an enzyme either side of optimum pH

It denatures

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68

What happens to enzymes when their concentration increases

Rate of reaction is faster as you increase concentration

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69

Why does rate of reaction increase when enzyme concentration increases

Higher chance of successful concentrations

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70

What happens when the enzyme concentration to rate graph plateau’s

Something other than active sites becomes the limiting factor

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71

What does an increase in SA mean in terms of reactions

Increased rate of reactions

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72

Define a competitive inhibitor

Molecules with a similar structure to substrate and can fit into active sites, preventing formation of enzyme substrate complexes

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73

Increase in substrate concentration does what too competitive inhibitors

Reduces their chance of forming an enzyme substrate complex

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74

Define a non competitive inhibitor

Molecules which bind to the enzyme at an alternative site, altering the shape of the active site

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75

What site does non-competitive inhibitors attach to

Allosteric site

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76

How does a non-competitive inhibitor denature the enzyme

By causing change to tertiary structure

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77

What is the effect of substrate concentrations on non-competitive inhibitors

Nothing, inhibitors always have an effect

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78

How do you calculate rate of reaction

Gradient of a graph

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79

What is an exopeptidase

Hydrolyses peptide bonds between amino acids, near the ends of a polypeptide to remove singular amino acids or dipeptides

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80

What are endopeptidases

Hydrolyse peptide bonds within a polypeptide forming smaller peptides to increase SA

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81

Name the control variables of an enzyme experiment testing temperature

pH, enzyme concnetration

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82

Explain the effects of increasing conc. of substrates on the rate without an inhibitor

More successful collisions between substrate and active site, forming more enzyme substrate complexes, so enzyme concentration is the limiting factor

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83

Explain why different enzymes are required to do different things

Enzymes are specific, and substrates are different shapes

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84

State the control variables for investigating pH of an enzyme

Substrate/enzyme concentration, temperature

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85

Name the monomer for proteins

Amino acids

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86

What elements do amino acids contain

Nitrogen, carbon, hydrogen, oxygen

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87

What groups does an amino acid contain

Amine (NH2), carboxyl (COOH) and residual (R)

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88

How many residual groups are there in nature

20

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89

What can proteins form in cells

Enzymes, cell membrane proteins, transport proteins, hormones

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90

What does the sequence, type and number of amino acids determine

Shape and function of proteins

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91

How many amino acids are there in nature

20

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92

Name the properties that change with the residual group

Molecule size, hydrophobic, hydrophilic and charge

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93

Describe formation of a peptide bond

Removal of an OH from the carboxylic group and a hydrogen removed from the amine group of the other amino acid

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94

What reaction forms a peptide bond

Condensation reaction

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95

Define a dipeptide

The condensation of two amino acids

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96

Define a polypeptide

The condensation of 3 or more amino acids

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97

What are the two main structures of a protein

Globular and fibrous

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98

Name a protein with a globular structure

Enzymes

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99

Name a protein with a fibrous structures

Keratin

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100

Describe globular proteins

Compact, roughly spherical and soluble proteins

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