A LEVEL BIO REVISION Flashcards
Number
Question
1
What is a light microscope used for?
2
What are the pros and cons of a light microscope?
3
What is a laser scanning confocal microscope used for?
4
Whatis a transmission electron microscope be used for?
5
What is a scanning electron microscope used for?
6
What are the pros and cons of an electron microscope?
7
What is the difference between a transmission and an scanning electron microscope?
8
What is the difference between light and electron microscopes?
9
What is an eye piece graticule?
10
What is a stage micrometer?
11
Why do we stain specimens?
12
What is differential staining?
13
What is the formula to calculate magnification?
14
What is the formula to calculate actual object size?
15
How do we work out image size?
16
What is magnification?
17
What is resolution?
18
What are the maximum resolutions of the different microscopes?
19
What is the maximum magnification of the different microscopes?
20
What are the main structures of all eukaryotic cells?
21
What is the structure and function of the nucleus?
22
What is the structure and function of the nucleolus?
23
What is the structure and function of the nuclear envelope?
24
What is the structure and function of the rough endoplasmic reticulum (RER)?
25
What is the structure and function of the smooth endoplasmic reticulum (SER)?
26
What is the structure and function of the Golgi apparatus?
27
What is the structure and function of the ribosomes?
28
What is the structure and function of the mitochondria?
29
What is the structure and function of the lysosomes?
30
What is the structure and function of the chloroplasts?
31
What is the structure and function of the plasma membrane?
32
What is the structure and function of the centrioles?
33
What is the structure and function of the cell wall?
34
What is the structure and function of the flagella?
35
What is the structure and function of the cillia?
36
Which structures are involved in the production of proteins?
37
What is the structure and function of the cytoskeleton?
38
What do prokaryotic and eukaryotic cells have in common?
39
What is different between prokaryotic and eukaryotic cells?
40
How do prokaryotes divide?
41
List out the elements that make up proteins.
42
Explain the polar nature of water.
43
What allows water molecules to have cohesive and adhesive properties?
44
Describe the structure of amylose, including the bonds involved and the shape.
45
Describe the structure of amylopectin, including the bonds involved and the shape.
46
State the two structures that make up starch.
47
State the reaction that breaks down maltose.
48
What is the reaction to join monosaccharides together?
49
What are the 3 types of polysaccharides that α-glucose can form?
50
What are the two monosaccharides that join up to make sucrose?
51
1,6 glycosidic bonds are found on ……..
52
β-glucose can only be found in ……..
53
How are the monosaccharides in cellulose arranged?
54
Based on the arrangement of cellulose molecules, explain why cell walls provide strength and support to plant cells.
55
What does the Benedict’s test test for?
56
Explain how a positive result is formed in Benedict’s test.
57
How can we test for starch?
58
How can we use a colorimeter to do a quantitative Benedict’s test?
59
What are the two parts that make up a carboxylic acid?
60
How many water molecule(s) is/are needed when breaking down a triglyceride?
61
What is another term for the condensation reaction that makes lipids?
62
What is the difference in structure between saturated and unsaturated lipids?
63
Why do oils contain unsaturated triglycerides rather than saturated?
64
What is the difference in structure between triglyceride and phospholipid?
65
Describe the phospholipid bilayer arrangement.
66
Describe 2 similarities and 1 difference between phospholipids and sterols.
67
Describe the steps in identifying lipids and state the positive result.
68
State the monomer of a protein.
69
What are the components that make up an amino acid?
70
Name the bond formed between two amino acids.
71
What is the primary structure of a protein?
72
What is the secondary structure of a protein?
73
What is the tertiary structure of a protein?
74
What is the quaternary structure of a protein?
75
State the bond involved in the primary structure of a protein.
76
Stat the bond involved in the secondary structure of a protein
77
State the bond involved in the tertiary structure of a protein.
78
State the bond involved in the quaternary structure of a protein.
79
Name the reaction that breaks down proteins.
80
What is the solution used to test for the presence of proteins?
81
Describe a positive result for proteins.
82
What is thin layer chromatography?
83
Based on what principles are the amino acids separated in TLC?
84
Why should the chromatography plate be only handled by the edges?
85
What are the three types of proteins?
86
Explain why insulin is soluble in blood.
87
What are prosthetic groups?
88
Give an example of a conjugated protein.
89
Compare the haem groups in haemoglobin and catalase.
90
How many haem groups do a haemoglobin contain?
91
Explain why keratin is relatively strong, inflexible and insoluble.
92
Briefly describe the structure of collagen.
93
What bonds do DNA/RNA polymerase catalyse?
94
Name the monomer of a nucleic acid.
95
State the five possible bases of a nucleotide.
96
State the three components to a DNA nucleotide.
97
The two strands of the double helix are …………. to each other.
98
Thymine, cytosine and uracil belong to a group of bases. Name the group.
99
Adenine and guanine belong to a group of bases. Name the group.
100
State the complementary base pairings.
101
State the number of hydrogen bonds formed between adenine and thymine/uracil.
102
State the number of hydrogen bonds formed between cytosine and guanine.
103
Why is DNA replication described as semi-conservative?
104
State the enzymes involved in DNA replication.
105
State the function of DNA polymerase.
106
State the function of DNA helicase.
107
The free nucleotides pair up with the exposed bases on the DNA strands based on …… (which principle?)
108
DNA polymerase can only build phosphodiester bonds on the daughter strand in a particular direction. What is this direction?
109
In which direction of the template strand does the DNA polymerase move in?
110
Define ‘genetic code’.
111
The genetic code is described as ‘degenerate’. What does that mean?
112
Define ‘gene’.
113
What is a codon?
114
What are the two differences between DNA and RNA?
115
Name the enzymes involved in transcription.
116
Why is the antisense strand needed even though it does not code for proteins?
117
What type of bond does mRNA have?
118
Even though DNA codes for proteins directly, why is mRNA needed to be made for making proteins?
119
How is rRNA involved in catalysing translation?
120
Which part of tRNA binds to the mRNA?
121
Name the amino acid that is always at the start of a protein.
122
Describe what happens to the amino acid chain to make it a fully functional protein.
123
State the two stages of protein synthesis.
124
Name the product of transcription.
125
Name the product of translation.
126
State the location where translation occurs.
127
What are the three main types of activities in cells that require energy?
128
What does ‘ATP’ stand for and what is it?
129
Draw the structure of ATP.
130
How does ATP release energy?
131
State 3 properties of ATP.
132
What are metabolic reactions?
133
What are anabolic reactions?
134
What are catabolic reactions?
135
What are enzymes?
136
Name the energy that is required to start a reaction.
137
What are enzymes’ effect on the activation energy of a reaction?
138
Name the area on the enzyme that binds to and reacts with the substrate.
139
The active site has a _____ shape to the substrate.
140
Name the two models used to illustrate enzyme actions.
141
Name the structure where the enzyme and substrate are bound together.
142
What is the difference between the lock-and-key model and the induced fit model?
143
Name an intracellular enzyme.
144
Name an extracellular enzyme.
145
Define the term ‘denaturation’.
146
Explain how an increase of temperature increases enzyme activity.
147
Explain how high temperatures can denature enzymes.
148
What is the temperature coefficient (Q10)?
149
How are the enzymes in organisms that live in cold environments adapted?
150
How are the enzymes in organisms that live in hot environments adapted?
151
How does a change in pH affect enzyme structure?
152
Explain why an increase in substrate concentration increases rate of reaction.
153
What does it mean by a ‘reversible’ inhibitor?
154
Most competitive inhibitors are reversible or irreversible?
155
Explain how Vmax of the enzyme can be unchanged in competitive inhibition.
156
What types of inhibitor does aspirin belong to?
157
Explain the difference between competitive and non-competitive inhibition mechanisms.
158
Explain how an increase in substrate concentration affects the rate of reaction in non-competitive inhibition.
159
State two examples of irreversible, non-competitive inhibitors for human use.
160
What is end-product inhibition?
161
How does ATP regulate its own production by end-product inhibition?
162
State the difference between cofactors and coenzymes.
163
From which chemical are cofactors derived from?
164
From which chemical are coenzymes derived from?
165
Name the cofactor found in amylase.
166
Name the cofactor invovled in photosynthesis.
167
Name the cofactor invovled in respiration.
168
State the difference between cofactors and prosthetic groups.
169
Name the prosthetic group in haemoglobin.
170
Name the prosthetic group in carbonic anhydrase.
171
What are the three ways that an enzyme can be activated by changing the tertiary structure?
172
Why is it important that some enzymes are produced in its inactive form?
173
What is an apoenzyme?
174
What is a holoenzyme?
175
What is the fluid mosaic model?
176
What is a glycolipid?
177
What is a glycoprotein?
178
State four functions of membranes at the surface of cells
179
State 3 functions of membranes within cells
180
The principal design of the plasma membrane consists of two layers; what name is given to these two layers?
181
Explain the orientation of phospholipids within the bilayer
182
Describe the function of glycoproteins and glycolipids in the phospholipid bilayer
183
Give 3 examples of intrinsic proteins
184
Channel proteins and carrier proteins have what main role within the membrane?
185
Describe the position and role of cholesterol in the membrane
186
Describe the structure of a phospholipid
187
Describe the effects of temperature on membrane structure
188
Describe the effects of ethanol on membrane structure
189
Explain why alcohol is used in antiseptic wipes.
190
Define the term diffusion.
191
Define the term facilitated diffusion
192
What is a channel protein?
193
What is a carrier protein?
194
What types of molecules can diffuse directly across the phospholipid bilayer?
195
Describe the movement of water across the phospholipid bilayer
196
State 5 factors that affect the rate of simple diffusion
197
Define the term active transport
198
Describe how carrier proteins are used in active transport
199
Define bulk transport and give two examples