Molecular Biology Flashcards

Molecules to metabolism, Water, Carbohydrates and lipids, Proteins, Enzymes, Structure of DNA and RNA, DNA replication, transcrption and translation, Cell respiration, Photosynthesis

1
Q

Define “molecular biology”

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2
Q

Compare the benefits of a reductionist vs. systems approach to studying biology

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3
Q

Recognize common functional groups

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4
Q
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4
Q

Draw skeletal molecular structures from full structure diagrams

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5
Q

Outline the number and type of bond carbon can form with other atoms

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6
Q

List the four major classes of carbon compounds used by living organisms

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7
Q

Define “metabolism” and “catalysis”

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8
Q

State the role of enzymes in metabolism

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9
Q

Define “anabolism”, “monomer”, and “polymer”

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10
Q

Describe condensation reactions

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11
Q

Using simple shapes to represent monomers, diagram a condensation reaction

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12
Q

Define “catabolism”

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13
Q

Contrast anabolism and catabolism

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14
Q

Describe hydrolysis reactions

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15
Q

Using simple shapes to represent monomers, diagram a hydrolysis reaction

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16
Q

Draw the molecules structure of urea

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17
Q

Describe how urea can be synthesized by living and artificial mechanisms

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18
Q

Draw the molecular diagram of ribose

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19
Q

Draw the molecular diagram of alpha-glucose

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20
Q

Draw the molecular diagram of a saturated fatty acid

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21
Q

Identify the carboxyl and methyl groups on a fatty acid

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22
Q

Draw the generalized structure of an amino acid

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23
Q

Label the amine group, carboxyl group, alpha carbon, and R group on an amino acid

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24
Q

Identify the four major classes of carbon compounds used by living organisms from four given diagrams (examples will include D-ribose, alpha glucose, beta glucose, triglycerides, phospholipids, and steroids)

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25
Q

State the generalized chemical formula for carbohydrates

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26
Q

Identify the following carbohydrates from molecules drawings: D-ribose, alpha glucose, beta glucose, cellulose, glycogen, amylose starch, and amylopeptin starch

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27
Q

Compare the relative amount of oxygen atoms in lipids to the amount in carbohydrates

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28
Q

Identify the following lipids from molecular drawings: triglycerides, phospholipids, and steroids

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29
Q

Define “vitalism”

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30
Q

Explain the role of urea in the falsification of vitalism

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31
Q
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31
Q

Describe the structure of an atom (in terms of protons, neutrons and electrons)

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32
Q

Contrast ion with atom

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33
Q

Define “anion” and “cation”

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34
Q

Contrast covalent, ionic, and hydrogen bonds

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35
Q

Write the molecular formula for water and draw the atomic structure of the molecule

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36
Q

Describe the cause effect of the polar nature of water

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37
Q

Describe where and how water is able to form hydrogen bonds

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38
Q

Contrast adhesion with cohesion

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39
Q

Outline an example of the cohesive property of water being of benefit to life

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40
Q

Outline an example of the adhesive property of water being of benefit to life

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41
Q

Explain three thermal properties of water that are useful to living organisms

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42
Q

Outline a benefit to life of water’s high specific heat capacity

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43
Q

Outline a benefit to water’s high latent heat of vaporization

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44
Q

Outline a benefit to life of water’s high boiling point

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45
Q

Explain why water is such a good solvent

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46
Q

List the types of molecules that water will dissolve

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47
Q

State that polar and ionic molecules are hydrophilic

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48
Q

State that non-polar, non-ionic molecules are hydrophobic

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49
Q

Given a diagram of a molecular structure, determine if the molecule is hydrophilic or hydrophobic

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50
Q

Compare the physical properties of methane and water

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51
Q

Explain why water and methane have different thermal properties based on their molecular structures

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52
Q

Explain sweating as a mechanism to cool the body

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53
Q

State if the following molecules are hydrophobic or hydrophilic: glucose, amino acids, cholesterol, fats, oxygen, and sodium chloride

A

Hydrophobic:

Hydrophilic:

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54
Q

Outline the mechanism of transport in the blood in the following molecules: glucose, amino acids, cholesterol, fats, oxygen, and sodium chloride

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55
Q

State why scientists cannot prove without a doubt that hydrogen bonds exist between water molecules.

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56
Q

Define “monosaccharide”, “disaccharide” and “polysaccharide”

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57
Q

List three examples of monosaccharides

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58
Q

List three examples of disaccharides

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59
Q

List three examples of polysaccharides

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60
Q

Use molecular diagrams to draw the formation of maltose from two glucose monomers

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61
Q

Explain a condensation reaction connecting two monosaccharides in the formation of a disaccharide

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62
Q

Describe the differences between saturated and unsaturated (mono- or poly-) fatty acids

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63
Q

Describe the differences between cis- and trans- fatty acids

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64
Q

Outline the difference between fats and oils

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65
Q

State two functions of triglycerides

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65
Q

Explain a condensation reaction connecting fatty acids and glycerol to form a triglyceride

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66
Q

Explain the energy storage of lipids compared to that of carbohydrates

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66
Q

State the structural difference between alpha and beta glucose

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67
Q

Contrast the structure and functions of cellulose, amylose, amylopectin and glycogen

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68
Q

Discuss the relationship between saturated fatty acid and trans-unsaturated fat intake and rates of coronary heart disease

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69
Q

Define evaluation in respect to evidence from and methods of research

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70
Q

Outline the manner in which the implications of research can be assessed

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70
Q

Outline the manner in which the limitations of research can be assessed

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71
Q

Evaluate a given health claim made about lipids

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72
Q

Demonstrate use of JMol to view molecular structures, including changing image size, rotating the image and changing the style of the molecular model

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73
Q

Identify carbon, hydrogen and oxygen atoms by color

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74
Q

Determine BMI using a nomogram

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75
Q

Outline effects of a BMI that is too high or too low.

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75
Q

Calculate BMI using the formula

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76
Q

Describe how the effect of lipids on health can be assessed scientifically

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77
Q

Describe polypeptide chain formation in terms of the formation of peptide bonds and condensation reactions

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78
Q

Determine the number of peptide bonds given the number of amino acids in a polypeptide

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79
Q

Define dipeptide, oligopeptides and polypeptide

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80
Q

State the number of amino acids used by living organisms to make polypeptides

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81
Q

Given an image of an amino acid, classify the amino acid chemical properties based on R group properties

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82
Q

Outline the role vitamin C plays in the conversion of proline to hydroxyproline

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83
Q

Calculate the possible number of amino acid sequences given n number of amino acids

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84
Q

Outline the relationship between genes and polypeptides

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85
Q

Outline the structure and function of three example proteins composed of two or more polypeptides linked together

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86
Q

Contrast the structure of globular proteins with the structure of fibrous proteins

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87
Q

Describe the structure of membrane bound globular proteins

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88
Q

Contrast the generalized function of globular proteins with generalized function of fibrous proteins

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89
Q

List ten functions of proteins in a cell or organism

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90
Q

Describe the function of enzyme proteins

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91
Q

Describe the function of hormone proteins.

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92
Q

Describe the function of immunoglobulin proteins

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93
Q

Describe the function of pigment proteins

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94
Q

Describe the function of structural proteins

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95
Q

Define proteome

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96
Q

Contrast proteome with genome

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97
Q

State the function of each of the following proteins: rubisco, insulin, immunoglobulin, rhodopsin, collagen, spider silk, actin, myosin, casein, hemoglobin, acetylcholine receptor, oxytocin, prolactin, ferritin, billirubin, fibrinogen, transferrin and albumin

A

Rubisco:

Insulin:

Immunoglobin:

Rhodopsin:

Collagen:

Spider silk:

Actin:

Myosin:

Casein:

Hemoglobin:

Acetylcholine receptor:

Oxytocin:

Prolactin:

Ferritin:

Bilirubin:

Fibrinogen:

Transferrin:

Albumin:

98
Q

Define “denaturation”

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99
Q

Outline the effect of heat and pH on protein structure

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100
Q

Draw peptide bond formation in a condensation reactions

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101
Q

Explain the trend of organisms assembly of polypeptides from the same amino acids

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102
Q

Describe a discrepancy of the trend of all organisms using the same amino acids to assemble polypeptides

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103
Q

State the relationship between enzyme substrate and enzyme active site

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104
Q

Explain the relationship between enzyme structure and enzyme specificity, including the role of the active site

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105
Q

Explain the role of random collisions in the binding of the substrate with the enzyme active site

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106
Q

Outline the three stages of enzyme activity

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107
Q

Describe the induced fit model of enzyme action

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107
Q

Explain how temperature affects the rate of enzyme activity

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108
Q

Draw a graph of depicting the effect of temperature on the rate of enzyme activity

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109
Q

Explain how pH affects the rate of enzyme activity

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110
Q

Draw a graph of depicting the effect of pH on the rate of enzyme activity

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111
Q

Identify the optimum temperature or pH for enzyme activity on a graph

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112
Q

Explain how substrate concentration affects the rate of enzyme activity

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112
Q

Draw a graph of depicting the effect of substrate concentration on the rate of enzyme activity

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112
Q

State the effect of denaturation on enzyme structure and function

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113
Q

List industries that use commercially useful enzymes

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114
Q

Explain how and why industrial enzymes are often immobilized

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115
Q

State the source of the lactase enzyme used in food processing

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116
Q

State the reaction catalyzed by lactase

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117
Q

Outline four reasons for using lactase in food processing

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118
Q

Identify and manipulated, responding and controlled variables in descriptions of experiments testing the activity of enzymes

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119
Q

Describe three techniques for measuring the activity of an example enzyme

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120
Q

State the two types of nucleic acid

A

DNA and RNA

121
Q

Outline the parts of a nucleotide

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122
Q

Identify and label carbons by number (for example, C1, C2, C3) on a nucleotide drawing

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123
Q

Explain how nucleotides can connect to form a nucleic acid polymer

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124
Q

State the names of the nitrogenous bases found in DNA and RNA.

A

Adenine, Thymine (DNA) / Uracil (RNA), Guanine, Cytosine,

125
Q

Identify nitrogenous bases as either a pyrimidine or purine

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126
Q

State the complementary base pairing rules

A

Adenine - Thymine
Cytosine - Guanine

127
Q

Compare the structure of DNA and RNA

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128
Q

Define antiparallel in relation to DNA structure

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129
Q

Outline the formation of a DNA double helix by hydrogen bonding between nitrogenous bases

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130
Q

Identify the four bases of DNA based on the numbers of rings (purines or pyrimidines) and the number of hydrogen bonds it can form.

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131
Q

State the number of nitrogenous bases per complete turn of the DNA double helix

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132
Q

Outline the role of Chargaff, Watson, Crick, Franklin and Wilkins in the discovery of DNA structure

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133
Q

Explain how Watson and Crick used model building to determine the structure of DNA

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134
Q

Draw the basic structure of a single nucleotide (using circle, pentagon and rectangle)

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135
Q

Draw a simple diagram of the structure of RNA

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136
Q

Draw a simple diagram of the structure of DNA

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137
Q

Identify and label the 5’ and 3’ ends on a DNA or RNA diagram

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138
Q

List types of models used in science

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139
Q

State a common feature of models in science

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140
Q

List ways in which models are different from the structure or process it represents

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141
Q

Describe the meaning of “semi-conservative” in relation to DNA replication

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142
Q

Explain the role of complementary base pairing in DNA replication

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143
Q

State why DNA strands must be separated prior to replication

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144
Q

Outline two functions of helicase

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145
Q

State the role of the origin of replication in DNA replication

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145
Q

Describe the movement of DNA polymerase along the DNA template strand

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146
Q

Contrast the number of origins in prokaryotic cells to the number in eukaryotic cells

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147
Q

Describe the action of DNA polymerase III in pairing nucleotides during DNA replication

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148
Q

Define “transcription”

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149
Q

Outline the process of transcription, including the role of RNA polymerase and complementary base pairing

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150
Q

Identify the sense and antisense strands of DNA given a diagram of translation

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151
Q

Define “translation”

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152
Q

State the location of translation in the cell

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153
Q

Outline the role of messenger RNA in translation

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154
Q

Define “codon”, “redundant”, and “degenerate” as related to the genetic code

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155
Q

Explain how using a 4 letters nucleic acid “language” can code for a “language” of 20 amino acid letters in proteins

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156
Q

Outline the role of complementary base pairing between mRNA and tRNA in translation

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157
Q

Outline the process of the PCR

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158
Q

Explain the use of Taq DNA polymerase in the PCR

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158
Q

Outline the source and use of pharmaceutical insulin prior to the use of gene transfer technology

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159
Q

Outline the benefits of using gene transfer technology in the production of pharmaceutical insulin

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160
Q

Use a genetic code table to deduce the mRNA codon(s) given the name of an amino acid

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161
Q

Compare dispersive, conservative and semi-conservative replication

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162
Q

Predict experimental results in the Meselson and Stahl experiment if DNA replication was dispersive, conservative or semi-conservative

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163
Q

Use a genetic code table to determine the amino acid sequence coded for by a given antisense DNA sequence or an mRNA sequence.

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164
Q

Deduce the antisense DNA base sequence that was transcribed to produce a given mRNA sequence

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165
Q

Describe the procedure of the Meselson and Stahl experiment

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166
Q

Explain how the Meselson and Stahl experiment demonstrated semi-conservative DNA replication

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167
Q

State the types of organic compounds used in cellular respiration by animals and plants

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167
Q

​Define “cell respiration”

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167
Q

Outline energy transfer in the formation and use of ATP

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168
Q

State the reaction for cellular respiration

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169
Q

State three example uses of cellular energy

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170
Q

Define “anaerobic respiration”

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170
Q

State three reasons why cellular respiration must be continuously performed by all cells

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170
Q

List three situations in which anaerobic respiration is useful.

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171
Q

Compare anaerobic respiration in yeasts and humans

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171
Q

​State the location of aerobic respiration.

A
172
Q

Compare the total amount of ATP made from anaerobic and aerobic respiration

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173
Q

Outline how anaerobic respiration in yeast is used in baking

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174
Q

Outline how anaerobic respiration in yeast is used in ethanol production

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175
Q

State the condition in which humans would perform anaerobic respiration

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176
Q

Outline production of lactate in humans during anaerobic respiration

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177
Q

Outline the use of a respirometer to measure cellular respiration rate

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178
Q

State the chemical equation for photosynthesis

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178
Q

List ethical questions that must be considered before using animals in experiments

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179
Q

Define “photosynthesis”

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180
Q

State the relationship between wavelength and energy

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181
Q

State that the oxygen produced in photolysis is a waste product of photosynthesis

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181
Q

Define “visible light”

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182
Q

State the range of wavelengths that fall within the visible spectrum

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183
Q

Define “pigment”

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184
Q

State the primary and accessory pigments found in chloroplasts

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185
Q

Explain why plants are green.

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186
Q

​Define “photolysis”

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187
Q

State the equation for photolysis

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188
Q

State the energy conversion that occurs during photosynthesis

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189
Q

Define “limiting factor”

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190
Q

Explain how the following factors limit the rate of photosynthesis: temperature, light intensity, and CO2 concentration

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191
Q

State that (some) prokaryotes, algae and plants carry out photosynthesis

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192
Q

Define and state evidence for the “Great Oxidation Event”

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193
Q

Describe the shape of the curve for an absorption spectrum

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193
Q

Distinguish between an action spectrum and an absorption spectrum

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194
Q

​List mechanism for measuring the rate of photosynthesis

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195
Q

Describe the shape of the curve for an action spectrum

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196
Q

Outline the process of separating pigments using chromatography

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197
Q

Calculate the Rf value for pigments using pigment chromatography

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198
Q

Define independent variable, controlled variable and responding variable

A