Strathallan Higher Human Biology Unit 1

Front 1

Differentiation

Back 1

Unspecialised cells become specialised

Front 2

Somatic cell

Back 2

Body cells that divide by mitosis

Front 3

Stem cell

Back 3

Unspecialised somatic cells that can divide to make copies of themselves and/or differentiate into specialised cells

Front 4

How does a stem cell differentiate into one type of cell rather than another?

Back 4

Certain genes are switched on and expressed

Front 5

Name the three components of a nucleotide of DNA.

Back 5

1. Deoxyribose sugar

2. Phosphate

3. Base

Front 6

Name the four bases in DNA

Back 6

1. Adenine

2. Thymine

3. Cytosine

4. Guanine

Front 7

State the base pairing rule

Back 7

A - T

C - G

Front 8

What types of bond hold the two DNA strands together?

Back 8

Hydrogen

Front 9

Which part of the DNA strand is the 3' end?

Back 9

Deoxyribose

Front 10

What is meant by the term anti-parallel in DNA?

Back 10

The two sugar-phosphate backbones run in opposite directions

Front 11

What is a chromosome?

Back 11

Tightly coiled DNA packaged with proteins

Front 12

Describe the stages involved in DNA replication

Back 12

1. DNA is unwound and unzipped

2. Primer attaches to the exposed bases

3. DNA polymerase adds nucleotides

4. Nucleotides added at the 3' end

5. One strand copied continuously, the other in fragments

6. Ligase enzyme joins the fragments together

Front 13

Phenotype

Back 13

A protein produced as a result of the expression of genes

Front 14

State three differences between DNA and RNA

Back 14

1. DNA has deoxyribose sugar, RNA has ribose sugar

2. DNA is double stranded,

RNA is single stranded

2. DNA has thymine,

RNA has uracil

Front 15

Name the four main body tissues

Back 15

1. Epithelial

2. Connective

3. Muscle

4. Nervous

Front 16

What makes up a ribosome?

Back 16

1. rRNA

2. Protein

Front 17

Describe the stages of transcription

Back 17

1. RNA polymerase unwinds and unzips DNA

2. RNA nucleotides bind to complementary bases on DNA

3. A-U, C-G

4. RNA polymerase joins RNA nucleotides together

5. Introns removed

6. Exons joined together by splicing

7. Primary transcript formed

Front 18

Describe the stages of translation

Back 18

1. mRNA attaches to ribosome

2. mRNA contains codons (3 bases)

3. tRNA attaches to a specific amino acid

4. tRNA contains an anti-codon

5. Anti-codon binds to codon

6. Peptide bond forms between amino acids

7. Start codon begins protein, stop codon ends it

Front 19

Multipotent stem cell

Back 19

A cell that can differentiate into any cell type within that tissue (eg tissue stem cells)

Front 20

Pluripotent stem cell

Back 20

A cell that can differentiate into any cell type (eg embryonic stem cells)

Front 21

Germ line cell

Back 21

A cell that gives rise to sperm and egg

Front 22

What two types of cell division do germ line cells carry out?

Back 22

1. Mitosis

2. Meiosis

Front 23

Name two therapeutic uses of stem cells

Back 23

1. Corneal transplants

2. Skin grafts

Front 24

Why are stem cells used as model cells?

Back 24

1. To test drugs on

2. To investigate how diseases develop

Front 25

Tumour

Back 25

A mass of abnormal cells

Front 26

If cancer cells fail to attach to each other, they can spread through the body to form...

Back 26

Secondary tumours

Front 27

Codon

Back 27

Three bases on mRNA (code for a specific amino acid)

Front 28

Codon

Back 28

Three bases on mRNA (code for a specific amino acid)

Front 29

Anticodon

Back 29

Three bases on tRNA

Front 30

Codon

Back 30

Three bases on mRNA (code for a specific amino acid)

Front 31

Anticodon

Back 31

Three bases on tRNA

Front 32

Ribosome

Back 32

Site of protein synthesis

Front 33

Amino acid

Back 33

Building block of a protein

Front 34

Polypeptide

Back 34

A protein, made up of a long sequence of amino acids

Front 35

Primary transcript

Back 35

mRNA containing both introns and exons

Front 36

Give two examples of post-translational modification

Back 36

1. Cutting or combining of polypeptide chains

2. Adding phosphate or carbohydrate groups to the protein

Front 37

State three ways in which proteins are held in a 3D shape

Back 37

1. Peptide bonds

2. Hydrogen bonds

3. Interactions between amino acids

Front 38

State three ways in which proteins are held in a 3D shape

Back 38

1. Peptide bonds

2. Hydrogen bonds

3. Interactions between amino acids

Front 39

Substitution mutation

Back 39

Replacing one DNA nucleotide with another

Front 40

State three ways in which proteins are held in a 3D shape

Back 40

1. Peptide bonds

2. Hydrogen bonds

3. Interactions between amino acids

Front 41

Substitution mutation

Back 41

Replacing one DNA nucleotide with another

Front 42

Insertion mutation

Back 42

Adding a nucleotide to a DNA sequence

Front 43

State three ways in which proteins are held in a 3D shape

Back 43

1. Peptide bonds

2. Hydrogen bonds

3. Interactions between amino acids

Front 44

Substitution mutation

Back 44

Replacing one DNA nucleotide with another

Front 45

Insertion mutation

Back 45

Adding a nucleotide to a DNA sequence

Front 46

Deletion mutation

Back 46

Taking away a nucleotide from a DNA sequence

Front 47

State three ways in which proteins are held in a 3D shape

Back 47

1. Peptide bonds

2. Hydrogen bonds

3. Interactions between amino acids

Front 48

Substitution mutation

Back 48

Replacing one DNA nucleotide with another

Front 49

Insertion mutation

Back 49

Adding a nucleotide to a DNA sequence

Front 50

Deletion mutation

Back 50

Taking away a nucleotide from a DNA sequence

Front 51

Missense

Back 51

Replacing one amino acid codon with another

Front 52

State three ways in which proteins are held in a 3D shape

Back 52

1. Peptide bonds

2. Hydrogen bonds

3. Interactions between amino acids

Front 53

Substitution mutation

Back 53

Replacing one DNA nucleotide with another

Front 54

Insertion mutation

Back 54

Adding a nucleotide to a DNA sequence

Front 55

Deletion mutation

Back 55

Taking away a nucleotide from a DNA sequence

Front 56

Missense

Back 56

Replacing one amino acid codon with another

Front 57

Nonsense mutation

Back 57

Replacing an amino acid codon with a stop codon

Front 58

State three ways in which proteins are held in a 3D shape

Back 58

1. Peptide bonds

2. Hydrogen bonds

3. Interactions between amino acids

Front 59

Substitution mutation

Back 59

Replacing one DNA nucleotide with another

Front 60

Insertion mutation

Back 60

Adding a nucleotide to a DNA sequence

Front 61

Deletion mutation

Back 61

Taking away a nucleotide from a DNA sequence

Front 62

Missense

Back 62

Replacing one amino acid codon with another

Front 63

Nonsense mutation

Back 63

Replacing an amino acid codon with a stop codon

Front 64

Splice site mutation

Back 64

Creating or destroying the codons for splicing

Front 65

State three ways in which proteins are held in a 3D shape

Back 65

1. Peptide bonds

2. Hydrogen bonds

3. Interactions between amino acids

Front 66

Substitution mutation

Back 66

Replacing one DNA nucleotide with another

Front 67

Insertion mutation

Back 67

Adding a nucleotide to a DNA sequence

Front 68

Deletion mutation

Back 68

Taking away a nucleotide from a DNA sequence

Front 69

Missense

Back 69

Replacing one amino acid codon with another

Front 70

Nonsense mutation

Back 70

Replacing an amino acid codon with a stop codon

Front 71

Splice site mutation

Back 71

Creating or destroying the codons for splicing

Front 72

Frame shift mutation

Back 72

A mutation that means all codons downstream are out of phase

Front 73

State three ways in which proteins are held in a 3D shape

Back 73

1. Peptide bonds

2. Hydrogen bonds

3. Interactions between amino acids

Front 74

Substitution mutation

Back 74

Replacing one DNA nucleotide with another

Front 75

Insertion mutation

Back 75

Adding a nucleotide to a DNA sequence

Front 76

Deletion mutation

Back 76

Taking away a nucleotide from a DNA sequence

Front 77

Missense

Back 77

Replacing one amino acid codon with another

Front 78

Nonsense mutation

Back 78

Replacing an amino acid codon with a stop codon

Front 79

Splice site mutation

Back 79

Creating or destroying the codons for splicing

Front 80

Frame shift mutation

Back 80

A mutation that means all codons downstream are out of phase

Front 81

Deletion chromosome mutation

Back 81

Loss of a segment of a chromosome

Front 82

State three ways in which proteins are held in a 3D shape

Back 82

1. Peptide bonds

2. Hydrogen bonds

3. Interactions between amino acids

Front 83

Substitution mutation

Back 83

Replacing one DNA nucleotide with another

Front 84

Insertion mutation

Back 84

Adding a nucleotide to a DNA sequence

Front 85

Deletion mutation

Back 85

Taking away a nucleotide from a DNA sequence

Front 86

Missense

Back 86

Replacing one amino acid codon with another

Front 87

Nonsense mutation

Back 87

Replacing an amino acid codon with a stop codon

Front 88

Splice site mutation

Back 88

Creating or destroying the codons for splicing

Front 89

Frame shift mutation

Back 89

A mutation that means all codons downstream are out of phase

Front 90

Deletion chromosome mutation

Back 90

Loss of a segment of a chromosome

Front 91

Duplication chromosome mutation

Back 91

Repeat of a segment of a chromosome

Front 92

State three ways in which proteins are held in a 3D shape

Back 92

1. Peptide bonds

2. Hydrogen bonds

3. Interactions between amino acids

Front 93

Translocation chromosome mutation

Back 93

The rearrangement of chromosomal material between two or more chromosomes

Front 94

Substitution mutation

Back 94

Replacing one DNA nucleotide with another

Front 95

Insertion mutation

Back 95

Adding a nucleotide to a DNA sequence

Front 96

Deletion mutation

Back 96

Taking away a nucleotide from a DNA sequence

Front 97

Missense

Back 97

Replacing one amino acid codon with another

Front 98

Nonsense mutation

Back 98

Replacing an amino acid codon with a stop codon

Front 99

Splice site mutation

Back 99

Creating or destroying the codons for splicing

Front 100

Frame shift mutation

Back 100

A mutation that means all codons downstream are out of phase

Front 101

Deletion chromosome mutation

Back 101

Loss of a segment of a chromosome

Front 102

Duplication chromosome mutation

Back 102

Repeat of a segment of a chromosome

Front 103

State three ways in which proteins are held in a 3D shape

Back 103

1. Peptide bonds

2. Hydrogen bonds

3. Interactions between amino acids

Front 104

Translocation chromosome mutation

Back 104

The rearrangement of chromosomal material between two or more chromosomes

Front 105

Bioinformatics

Back 105

The use of computer technology to identify DNA sequences

Front 106

Substitution mutation

Back 106

Replacing one DNA nucleotide with another

Front 107

Insertion mutation

Back 107

Adding a nucleotide to a DNA sequence

Front 108

Deletion mutation

Back 108

Taking away a nucleotide from a DNA sequence

Front 109

Missense

Back 109

Replacing one amino acid codon with another

Front 110

Nonsense mutation

Back 110

Replacing an amino acid codon with a stop codon

Front 111

Splice site mutation

Back 111

Creating or destroying the codons for splicing

Front 112

Frame shift mutation

Back 112

A mutation that means all codons downstream are out of phase

Front 113

Deletion chromosome mutation

Back 113

Loss of a segment of a chromosome

Front 114

Duplication chromosome mutation

Back 114

Repeat of a segment of a chromosome

Front 115

State three ways in which proteins are held in a 3D shape

Back 115

1. Peptide bonds

2. Hydrogen bonds

3. Interactions between amino acids

Front 116

Translocation chromosome mutation

Back 116

The rearrangement of chromosomal material between two or more chromosomes

Front 117

Bioinformatics

Back 117

The use of computer technology to identify DNA sequences

Front 118

Systematics

Back 118

Compares the human genome with genomes of other species

Front 119

Substitution mutation

Back 119

Replacing one DNA nucleotide with another

Front 120

Insertion mutation

Back 120

Adding a nucleotide to a DNA sequence

Front 121

Deletion mutation

Back 121

Taking away a nucleotide from a DNA sequence

Front 122

Missense

Back 122

Replacing one amino acid codon with another

Front 123

Nonsense mutation

Back 123

Replacing an amino acid codon with a stop codon

Front 124

Splice site mutation

Back 124

Creating or destroying the codons for splicing

Front 125

Frame shift mutation

Back 125

A mutation that means all codons downstream are out of phase

Front 126

Deletion chromosome mutation

Back 126

Loss of a segment of a chromosome

Front 127

Duplication chromosome mutation

Back 127

Repeat of a segment of a chromosome

Front 128

State three ways in which proteins are held in a 3D shape

Back 128

1. Peptide bonds

2. Hydrogen bonds

3. Interactions between amino acids

Front 129

Translocation chromosome mutation

Back 129

The rearrangement of chromosomal material between two or more chromosomes

Front 130

Bioinformatics

Back 130

The use of computer technology to identify DNA sequences

Front 131

Systematics

Back 131

Compares the human genome with genomes of other species

Front 132

Describe the process of PCR

Back 132

1. DNA heated (to separate strands)

2. DNA cooled (to allow primers to bind)

3. DNA heated (to optimise DNA polymerase which replicates the DNA)

Front 133

Substitution mutation

Back 133

Replacing one DNA nucleotide with another

Front 134

Insertion mutation

Back 134

Adding a nucleotide to a DNA sequence

Front 135

Deletion mutation

Back 135

Taking away a nucleotide from a DNA sequence

Front 136

Missense

Back 136

Replacing one amino acid codon with another

Front 137

Nonsense mutation

Back 137

Replacing an amino acid codon with a stop codon

Front 138

Splice site mutation

Back 138

Creating or destroying the codons for splicing

Front 139

Frame shift mutation

Back 139

A mutation that means all codons downstream are out of phase

Front 140

Deletion chromosome mutation

Back 140

Loss of a segment of a chromosome

Front 141

Duplication chromosome mutation

Back 141

Repeat of a segment of a chromosome

Front 142

DNA probe

Back 142

Short, single strands of DNA that detect the presence of specific DNA sequences

Front 143

Anabolic pathway

Back 143

A pathway that is biosynthetic (making bigger molecules) and requires energy

Front 144

Anabolic pathway

Back 144

A pathway that is biosynthetic (making bigger molecules) and requires energy

Front 145

Catabolic pathway

Back 145

A pathway that involves the breakdown of molecules and releases energy

Front 146

Anabolic pathway

Back 146

A pathway that is biosynthetic (making bigger molecules) and requires energy

Front 147

Catabolic pathway

Back 147

A pathway that involves the breakdown of molecules and releases energy

Front 148

Induced fit

Back 148

When a substrate approaches the enzyme, it causes a change in the shape of the active site that allows the substrate to bind

Front 149

Activation energy

Back 149

The energy required for an enzyme-catalysed reaction to occur

Front 150

Competitive inhibitor

Back 150

Binds to the active site, blocking the substrate from binding

Front 151

Competitive inhibitor

Back 151

Binds to the active site, blocking the substrate from binding

Front 152

Non-competitive inhibitor

Back 152

Bonds away from the active site but causes a permanent change in the shape of the active site

Front 153

Feedback inhibition

Back 153

End product binds to and inhibits an enzyme that catalysed a reaction early in the pathway

Front 154

State two functions of ATP

Back 154

1. Providing energy

2. Phosphorylation of molecules

Front 155

What is the end product of glycolysis?

Back 155

Pyruvate

Front 156

State two functions of ATP

Back 156

1. Providing energy

2. Phosphorylation of molecules

Front 157

What is the end product of glycolysis?

Back 157

Pyruvate

Front 158

Name the three stages of aerobic respiration

Back 158

1. Glycolysis

2. Citric acid cycle

3. Electron transport chain

Front 159

What happens in the energy investment stage of glycolysis?

Back 159

ATP is used up

Front 160

What happens in the energy pay-off stage of glycolysis?

Back 160

ATP is produced

Front 161

What happens in the energy pay-off stage of glycolysis?

Back 161

ATP is produced

Front 162

Name an enzyme in glycolysis that produces an intermediate substance in an irreversible step

Back 162

Phosphofructokinase

Front 163

What happens in the energy pay-off stage of glycolysis?

Back 163

ATP is produced

Front 164

Name an enzyme in glycolysis that produces an intermediate substance in an irreversible step

Back 164

Phosphofructokinase

Front 165

How is acetyl co-enzyme A produced?

Back 165

Pyruvate >> acetyl

Acetyl + co-enzyme A >> acetyl co-enzyme A

Front 166

What happens in the energy pay-off stage of glycolysis?

Back 166

ATP is produced

Front 167

Name an enzyme in glycolysis that produces an intermediate substance in an irreversible step

Back 167

Phosphofructokinase

Front 168

How is acetyl co-enzyme A produced?

Back 168

Pyruvate >> acetyl

Acetyl + co-enzyme A >> acetyl co-enzyme A

Front 169

How is citric acid produced?

Back 169

oxaloacetate + acetyl co-enzyme A >> citric acid

Front 170

What happens in the energy pay-off stage of glycolysis?

Back 170

ATP is produced

Front 171

Name an enzyme in glycolysis that produces an intermediate substance in an irreversible step

Back 171

Phosphofructokinase

Front 172

How is acetyl co-enzyme A produced?

Back 172

Pyruvate >> acetyl

Acetyl + co-enzyme A >> acetyl co-enzyme A

Front 173

How is citric acid produced?

Back 173

oxaloacetate + acetyl co-enzyme A >> citric acid

Front 174

Describe what happens during the citric acid cycle

Back 174

1. Citric acid is produced

2. ATP is produced

3. Carbon dioxide is released

4. NADH/FADH is produced

5. Oxaloacetate is regenerated

Front 175

What happens in the energy pay-off stage of glycolysis?

Back 175

ATP is produced

Front 176

Name an enzyme in glycolysis that produces an intermediate substance in an irreversible step

Back 176

Phosphofructokinase

Front 177

How is acetyl co-enzyme A produced?

Back 177

Pyruvate >> acetyl

Acetyl + co-enzyme A >> acetyl co-enzyme A

Front 178

How is citric acid produced?

Back 178

oxaloacetate + acetyl co-enzyme A >> citric acid

Front 179

Describe what happens during the citric acid cycle

Back 179

1. Citric acid is produced

2. ATP is produced

3. Carbon dioxide is released

4. NADH/FADH is produced

5. Oxaloacetate is regenerated

Front 180

Name the enzyme that removes hydrogen ions and electrons from molecules

Back 180

Dehydrogenase

Front 181

Name the two co-enzymes that pick up hydrogen ions and electrons

Back 181

1. NADH

2. FADH2

Front 182

How is ATP made in the electron transport chain?

Back 182

1. High energy electrons are used to pump hydrogen ions across a membrane.

2. The hydrogen ions flow back through the membrane using the protein ATP synthase.

3. TP is synthesised.

Front 183

What is the final electron acceptor in aerobic respiration?

Back 183

Oxygen

Front 184

Name give respiratory substrates

Back 184

1. Glucose

2. Starch

3. Glycogen

4. Fat

5. Protein

Front 185

What is meant by 'conservation of resources'?

Back 185

ATP is only made when needed

Front 186

What is the function of creatine phosphate?

Back 186

It breaks down to release creatine and phosphate that is used to convert ADP to ADP

Front 187

Describe what happens in anaerobic respiration.

Back 187

1. Hydrogen from NADH is added to pyruvate to become lactic acid

2. This regenerates NAD which is needed for ATP production

Front 188

Describe what happens in anaerobic respiration.

Back 188

1. Hydrogen from NADH is added to pyruvate to become lactic acid

2. This regenerates NAD which is needed for ATP production

Front 189

Which type of muscle fibre is associated with aerobic respiration?

Back 189

Slow twitch

Front 190

Describe what happens in anaerobic respiration.

Back 190

1. Hydrogen from NADH is added to pyruvate to become lactic acid

2. This regenerates NAD which is needed for ATP production

Front 191

Which type of muscle fibre is associated with aerobic respiration?

Back 191

Slow twitch

Front 192

Which type of muscle fibre has lots of mitochondria?

Back 192

Slow twitch

Front 193

Which type of muscle fibre does not have a good blood supply?

Back 193

Fast twitch

Front 194

Which type of muscle fibre does not have a good blood supply?

Back 194

Fast twitch

Front 195

What type of events are fast twitch muscle fibres best for?

Back 195

Bursts of activity (eg sprinting, weight lifting)