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IB Molecular Biology Flashcards

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1
Q

What is an organic compound?

A

An organic compound is a compound that contains carbon and is found in living things

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2
Q

What are exceptions to the organic compounds? (4)

A

CN, CO, CO2, CaC2

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3
Q

What are Carbohydrates and what are their functions?

A
  • Most abundant organic compound found in nature, composed primarily of C,H and O atoms in a common ratio – (CH2O)n
  • Principally function as a source of energy (and as a short-term energy storage option)
  • Also important as a recognition molecule (e.g. glycoproteins) and as a structural component (part of DNA / RNA)
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4
Q

What are Lipids and what are their functions?

A
  • Non-polar, hydrophobic molecules which may come in a variety of forms (simple, complex or derived)
  • Lipids serve as a major component of cell membranes (phospholipids and cholesterol)
  • They may be utilized as a long-term energy storage molecule (fats and oils)
  • Also may function as a signaling molecule (steroids)
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5
Q

What are Nucleic acids and what are their functions?

A
  • Genetic material of all cells and determines the inherited features of an organism
  • DNA functions as a master code for protein assembly, while RNA plays an active role in the manufacturing of proteins
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6
Q

What are proteins and what are their functions?

A
  • Make over 50% of the dry weight of cells; are composed of C, H, O and N atoms (some may include S)
  • Major regulatory molecules involved in catalysis (all enzymes are proteins)
  • May also function as structural molecules or play a role in cellular signaling (transduction pathways)
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7
Q

What are Carbohydrates composed of?

A

Carbohydrates are composed of monomers called monosaccharides

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8
Q

Catabolism

A

breakdown of complex molecules into simpler molecules including the hydrolysis of macromolecules into monomers

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9
Q

Anabolism

A

synthesis of complex molecules from simpler molecules, including the formation of macromolecules from monomers using condensation reactions

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10
Q

Metabolism

A

web of all enzyme-catalyzed reactions in a cell or organism

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11
Q

four biochemical groups

A
  • carbohydrates
  • lipids
  • proteins
  • nucleic acids
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12
Q

Why is life based on carbon

A

-it can form four covalent bonds; creates stable molecules
-allows for a diversity of molecules (bonds easily)
Not very reactive
Very small

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13
Q

What are the elements in living organisms

A
  • hydrogen
  • oxygen
  • nitrogen
  • phosphorous
  • carbon
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14
Q

Monomers/Dimers/Polymers of Carbohydrates

A

monomer; monosaccharides
dimers; disaccharides
polymers; polysaccharides

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15
Q

Monomers/Dimers/Polymers of Lipids

A

monomers; glycerol, fatty acids, phosphate groups

dimers/polymers; triglycerides, phospholipids, steroids (FAT)

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16
Q

Monomers/Dimers/Polymers of Proteins

A

monomer; amino acids

dimer/polymer; polypeptides

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17
Q

Monomers/Dimers/Polymers of Nucleic Acids

A

monomer; nucleotide

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18
Q

What determines if a reaction occurs or not?

A
  • identity of colliding molecules
  • orientation of colliding molecules
  • speed/kinetic energy of molecules
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19
Q

Why do cells use enzymes?

A

to increase the likelihood that a successful collision will lead to a useful reaction

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20
Q

What are enzymes?

A

protein molecules with a specific shape that a react can fit into at the active site

  • act as catalysts
  • increase rate of reaction
  • lower activation energy
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21
Q

What explains the properties of water?

A
  • dipolarity

- hydrogen bonding

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22
Q

What makes water so special?

A

its polar and hydrogen bonds form between them

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23
Q

Why is water polar?

A

due to the unequal sharing of electrons within the water molecule that makes oxygen slightly negative and hydrogen slightly positive

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24
Q

Cohesive properties of water

A

Cohesion: attraction of water molecules to other water molecules
- due to hydrogen bonds that form between water molecules due to polarity

explains;

  • why water forms into droplets when it is spilt
  • why water has a surface tension that allows for some animals to walk/run on it
  • why water can move as a water column in the xylem
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25
Q

Thermal properties of water

A
  • high latent heat of vaporization
  • high specific heat capacity

explains;

  • water can absorb a great deal of heat (good for chemical reactions)
  • act as a coolant
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26
Q

Adhesive properties of water

A

Adhesion: is the formation of hydrogen bonds between the water molecules and F, N and O (attraction between unlike molecules)

explains;
why water sticks to the vascular tissue in plants (fight gravity!) and can be pulled up

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27
Q

Bonds formed during condensation reactions

A
  • ester bond (triglycerides)
  • glyosidic bond (maltose)
  • peptide bond (amino acids)
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28
Q

Hydrophilic

A
  • water loving

- polar substance

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29
Q

Hydrophobic

A
  • water hating

- non polar substance

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30
Q

Monosaccharides (4)

A
  • glucose
  • fructose
  • galactose
  • ribose
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31
Q

Disaccharides (3)

A
  • sucrose
  • maltose
  • lactose
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32
Q

Polysaccharides (3)

A
  • starch
  • cellulose
  • glycogen
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33
Q

What is the role and structure of Cellulose

A
  • major component of cell walls
  • helps give rigidity support to plant parts such as roots, stems and leaves

Structural polysaccharide in plants
B-glucose
1:4 glyosidic bond
Unlike starch, cellulose is very strong and prevents cells from bursting when they take excess water
Consists of long chains of glucose molecules

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34
Q

What is the role and location of Glycogen

A
  • animals stores excess glucose in this form

- stored in liver and muscle areas

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35
Q

What are the functions of Lipids

A
  • long term storage of energy
  • they are important components of the cell membrane
  • they are used as a heat insulator
  • can act as a shock absorber
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36
Q

What are the 3 main types of Lipid

A
  1. triglycerides (Fats + Oils)
  2. Phospholipids (components of cell membrane)
  3. Steroids (Cholesterol, progesterone, estrogen, testosterone)
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37
Q

What are Triglycerides composed of?

A

TRIGLYCERIDES;
tri: refers to 3 fatty acids chains

  • glycerol
  • fatty acids
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38
Q

What are Saturated fatty acids and where are they found?

A

if the bonds between carbon atoms are SINGLE
the fatty acids contain as much hydrogen as they possibly could

animal sources (red meats, milk, etc.)&raquo_space;> FATS

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39
Q

What are Unsaturated fatty acids and where are they found?

A

UNSATURATED FATTY ACIDS
when the fatty acids contain 1 or more DOUBLE BONDS
contains less hydrogen atoms than it could (unfulfilled)

Plants (Oil)

can be polyunsatured or monoundsatured

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40
Q

What does CIS and TRANS unsaturated Fatty acids refer to and what are their roles and uses?

A

CIS:(can be poly)
same side C=C bond
when hydrogen atoms are on the same side with respect to the double bond

TRANS:(can be poly)
-when the hydrogen atoms are on the opposite side with respect to the double bond

CIS= Healthy
Trans= unhealthy

cis-fatty acids cannot line next to each other, thats why the are lipid at room temperature
cis fatty acids are ‘slippery’ and will not clog arteries
Trans Fatty Acids
-hydrogenation of vegetable or fish oils
-modification of natural, healthy oils
-hydrogenation changes the shape of the oil
-trans fats are illegal
-turns it from liquid» solid

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41
Q

What are phospholipids?

A

these are modified triglycerides that have one fatty acid chain by a phosphate group

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42
Q

Scientific Evidence of trans unsaturated fats health risk

A

Coronary heart disease: arteries become blocked due to fatty deposits

High intake of trans fats
CHD: found in patients who take more cis unsaturated fatty acids

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43
Q

BMI formula

A

weight (kg)/[height (m)x height (m)]

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44
Q

How is energy stored in humans?

A
  • storing glucose as glycogen in liver and muscle cells

- storing triglyceride lipids within adipose (fat) cells

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45
Q

What are the functions of proteins? (4)

A
  • structural
  • catalytic
  • signaling
  • immunological
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46
Q

What is Rubisco?

A

short hand name for enzyme that catalyzes the first reaction of carbon fixing reactions of photosynthesis

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47
Q

What is Insulin?

A

a protein hormone produced by the pancreas that results in a decrease of blood sugar levels and an increase of sugar inside body cells

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48
Q

What is Immunoglobin?

A

an antibody that recognizes an antigen as part of the immune response

49
Q

What is Rhodopsin?

A

pigment found in eye retina for low light conditions

50
Q

What is Collagen?

A

main protein component of connective tissue which is in skin, tendons and ligaments

51
Q

What is Spider silk and what are its uses for spiders?

A

fibrous protein spun by spiders for webs, lines, nest building, hunting

52
Q

How do the proteins differ from each other?

A

Length: different # of amino acids
Types: different types
Order: different order

53
Q

Primary structure of protein

A
  • linear sequence of AAs
  • contains only peptide bonds
  • in nature: proteins are almost never found in this structure because they fold to produce more complex molecules
54
Q

Secondary structure of protein

A
  • the polypeptide chain folds to form: alpha helix or beta pleated sheet
    examples: keratin (alpha helix) and silk (beta pleated sheet)
  • these structures are held together by hydrogen bonds
55
Q

Tertiary structure of protein

A
  • alpha helix and beta pleated sheets fold into compact globules
  • the structures are held together by: hydrogen bonds, ionic bonds and disulphide bonds
  • example: enzymes
56
Q

Quaternary structure of protein

A
  • examples: hemoglobin, collagen, insulin

- held together by: hydrogen bonds, ionic bonds, disulphide bonds

57
Q

Fibrous Proteins

A

Shape: Long and narrow

Role: Structural (strength and support)

Solubility: Generally insoluble in water

Sequence: Repetitive amino acid sequence

Stability: Less sensitive to change in heat and pH

Examples
Collagen, myosin, fibrin, actin, keratin, elastin

58
Q

Globular Proteins

A

Shape: Rounded/spherical

Role: Functional (catalytic, transport, etc)

Solubility: Generally soluble in water

Sequence: Irregular amino acid sequence

Stability; More sensitive to change in heat, pH, etc

Examples:
Catalase, hemoglobin, lipase, insulin, immunoglobulin, DNA Polymerase,

59
Q

Protome

A

All of the proteins produced by a cell, tissue or organ in a human
- as cells can differentiate they don’t have to produce the same proteins to have the same genome

60
Q

How do Proteins Denature

A
  • proteins can denature by heat and pH environment alteration (bonds broken and proteins get broken down into simpler forms/become inactive)
  • each protein has an optimum temperature
61
Q

Enzyme function

A

-Speed up reactions, acting as a catalyst
Long chain of amino acids (globular protein in tertiary structure)
Substrate»>enzyme»>product

62
Q

Active site

A

A small region on the enzyme where the substrate binds to and the reaction takes place, enzymes are substrate specific

63
Q

What are Catalysts?

A

They increase the rate of reaction without themselves being being used up.

64
Q

Steps of enzymatic process (4)

A
  1. substrate enters active site
  2. enzyme-substrate complex is formed
  3. substrate is changed into a different chemical (product)
    at the end of the reaction, the product leaves the active site
  4. enzymes are never permanently modified, they can return into their original state, to be used over + over again
65
Q

What are the two enzymatic reaction theories?

A
  • Lock and key

- Induced Fit

66
Q

Describe the Lock and Key Hypothesis

A

The substrate molecular shape is the exact match to the enzyme’s active site
the substrate fits perfectly into the enzyme’s active site, the way a key fits into a lock. Each substrate has a particular corresponding enzyme

67
Q

Describe the Induced-Fit Hypothesis

A

The substrate binds to the enzyme’s active site
the once the enzyme changes shape to fit and hold the substrate

Once the substrate binds into distorted active site, the complex is formed. and makes or breaks substrate by force

68
Q

What are the factors affecting enzyme activity

A

Temperature
-as temperature increases so does enzyme activity
this is because:
molecules move faster (most often substrate moves around, but enzyme can as well) causing more of a chance for the enzyme and the substrate to find each other and bind
Optimum temperature
when the activity of an enzyme is at its greatest (any point beyond that the activity declines because they begin to break)

SUBSTRATE CONCENTRATION

Denaturation
change in the shape of an enzyme, for example:
-an active enzyme is tridimensional
-when it is heated it loses shape because heat causes the enzyme to twist and bend, and the hydrogen bonds to break
-this affects its activity to recognize the substrate (because of the change in the shape of the active site

69
Q

Stages of Denaturation

A
  • Quaternary Structure lost = protein subunits are dissociated
  • Tertiary structure lost = interaction between side chains of amino acids are lost (hydrogen bonds/ionic bonds)
  • Binary Structure lost = proteins lose patterns such as alpha helix and beta pleated sheet and become random coil configurations
  • Primary structure = the sequence of amino acids (peptide bonds) remains
70
Q

How does a change in pH affect enzyme activity?

A

each enzyme has an optimum pH

-change in pH could result in change in the shape of the enzyme (new shape may not be active)

71
Q 
Optimum pH and location of:
pepsin
amylase
lipase
lactase
A

Pepsin - PH2 (Stomach
Amylase - PH7 (mouth, small intestine, pancreas)
Lipase - PH8 (small intestine)
Lactase - PH7 (small intestine)

72
Q

Uses of immobilized enzymes

A
  • used as catalysts in industry
  • enzymes can be held in tiny pores on beads called calcium alginate (trapped there; immobilized) so enzymes can be recovered and reused in processes

-used in the production of lactose-free milk for lactose intolerant people (enzyme lactase is immobilized to break don’t lactose into glucose and galactose and digest it)

73
Q

What is the role, and structure of DNA

A

deoxyribose nucleic acid, code for life and all the functions in a living organism

  • a double stranded helix
  • sugar phosphate backbone
  • anti parallel
  • nitrogen containing
  • hydrogen bonding and phosphodiester bonds
  • found in nucleus
  • pentose sugar- deoxyribose
74
Q

What are the nucleotide bases and their subdivisions?

A

PURINE:

  • adenine
  • guanine

PYRAMIDINE:

  • thymine
  • cytosine
  • uracil (only in RNA)
75
Q

What is RNAs role and function?

A

Single stranded

Ribose sugar

Uracil (GCUA)

Nucleic Acid

Found in nucleus and outside of it (can travel out)

Has pentose sugar

76
Q

What is Semi conservative replication

A

Mechanism of DNA replication where two new copies of DNA are produced from an original DNA strand consisting of one of the original strands and one new strand

77
Q

What are the 3 types of RNA?

A
  • mRNA
  • rRNA
  • tRNA
78
Q

What are the replication theories? (3)

A
  • Conservative: parental DNA is conserved
  • Dispersive (fragmented) : mixture of old and new DNA within the same chromosome
  • Semi conservative
79
Q

mRNA function

A

messenger RNA. Copy of a gene, carries information to make a protein

80
Q

rRNA function

A

ribosomal RNA, component of ribosomes. Large and small subunit

81
Q

tRNA function

A

transfer RNA. Brings amino acids to ribosomes during protein synthesis, has a site for the AA to attach and an anticodon (determines which of the 20 AA’s is attached to the tRNA)

82
Q

What Enzymes are used in replication? (4)

A
  • DNA Helicase
  • DNA Polymerase I
  • DNA ligase
  • Single-stranded binding protein:
83
Q

DNA Helicases function

A

DNA Helicase: separates the two DNA strands before replication

84
Q

Function of:
DNA Polymerase I
DNA Polymerase II

A

DNA Polymerase I:
Removes the primer and replaces it with DNA

DNA POLYERMASE II; Synthesized new strand by adding nucleotides onto the primer in a 5’ to 3’ direction

85
Q

DNA Ligases function

A

DNA ligase: joins together short sections of the lagging strand (okazaki fragments)

86
Q

Single-stranded binding proteins function

A

Single-stranded binding protein: keeps the separated DNA strands apart during replication`

87
Q

What is Polymerase Chain Reaction

A

developed in 1970’s

  • artificial DNA replication
  • duplicates short segments of DNA
  • scientists can produce large quantities of DNA this way for study
  • used for forensics studies and paterntity testing
  • Process consists of fluctuating temperatures
88
Q

AEROBIC respiration equation

A

AEROBIC:
Normal form of respiration through breathing (muscular contraction)
Glucose + oxygen —–> carbon dioxide + water + energy (ATP)
C6H12O6 + 6O2——> 6CO2 + 6H2O + 36ATP

89
Q

ANAEROBIC: respiration

A

ANAEROBIC:
When the body is getting no oxygen from breathing, so the cell creates energy just with glucose (inefficient)
In humans: glucose —–> Lactic Acid + Energy
C6H12O6—–> 2C3H6O3 + 2 ATP

90
Q

alcoholic fermentation

A
  • yeast
  • produces ethanol, carbon dioxide
  • use of fermentation in baking and alochol production
91
Q

lactic acid fermentation

A

-organisms can respire without oxygen
-produce lactic acid by breaking down pyruvate
-e.g. during excersize
Lactic acid causes muscular fatigue and pain, forms crystals in the muscle tissue that makes the movement hard, toxic to body

OXYGEN DEBT: oxygen needed to break down lactic acid into carbon dioxide and water

92
Q

PHOTOSYNTHESIS equation

A

CO2 + H2O ——–> O2 + C6H12O6
Photosynthesis is the production of carbon compounds in cells using light energy

Oxygen is produced from the photolysis of water (splitting of light)

93
Q

what does chlorphyll do when hit by light (and why are plants green?)

A
  • its a green pigment; reflects green light and absorbs all other wavelengths of the visible light spectrum (red and blue are absobved and used for photosynthesis)
94
Q

LIMITING FACTORS OF PHOTOSYNTHESIS:

A

LIMITING FACTORS:
1. Temperature: has an optimum temperature, when it gets an higher, the rate goes down, as the plants begin to deteriorate

  1. Carbon Dioxide: reaches a max concentration, after there is no change in the rate
  2. Light Intensity: reaches a max intensity, after there is no change in the rate
95
Q

What is the structure of Lactose?

A

Beta Glucose 1-4 Galactose

96
Q

What is the structure of Maltose?

A

Alpha Glucose 1-4 Alpha Glucose

97
Q

What is the structure of Sucrose?

A

Alpha Glucose 1-4 Fructose

98
Q

What is the structure of Starch?

A

Alpha Glucose 1-4 Alpha Glucose chain

99
Q

What is the structure of Cellulose?

A

Beta Glucose 1-4 Beta Glucose chain

100
Q

Why is Cellulose indigestible by humans but digestible by cows?

A

Because it is composed of β-glucose, it is indigestible for most animals (lack the enzyme required to break it down), however, cows have special bacteria that allow them to break down cellulose

101
Q

What are the two forms of Starch?

A
  • amylose

- amylopectin

102
Q

What is the structure of Glycogen?

A

It is composed of α-glucose subunits linked together by both 1-4 linkages and 1-6 linkages

103
Q

What do LDLs do?

A

Low density lipoproteins (LDL) carry cholesterol from the liver to the rest of the body

104
Q

What do HDLs do?

A

High density lipoproteins (HDL) scavenge excess cholesterol and carry it back to the liver for disposal

105
Q

Role of Hemoglobin

A

A protein found in red blood cells that is responsible for the transport of oxygen

106
Q

Role of Cytochrome

A

A group of proteins located in the mitochondria and involved in the electron transport chain

107
Q

Role of Actin

A

Thin filaments involved in the contraction of muscle fibers

108
Q

Role of Myosin

A

Thick filaments involved in the contraction of muscle fibers

109
Q

Role of Glucagon

A

Protein produced by the pancreas that triggers an increase in blood glucose levels

110
Q

What are the roles of proteins in a cell? (7)

A 
Structure – e.g. collagen, spider silk
Hormones – e.g. insulin, glucagon
Immunity – e.g. immunoglobulins
Transport – e.g. hemoglobin
Sensation – e.g. rhodopsin
Movement – e.g. actin, myosin
Enzymes – e.g. Rubisco, catalase

SHITs ME

111
Q

Why can water dissolve polar substances?

A

The polar attraction of large quantities of water molecules can sufficiently weaken intramolecular forces (such as ionic bonds) and result in the dissociation of the atoms

The slightly charged regions of the water molecule surround atoms of opposing charge, forming dispersive hydration shells

112
Q

What determines the primary structure of a protein?

A

The order of the amino acid sequence is called the primary structure and determines the way the chain will fold

113
Q

Into which two configurations will amino acid sequences fold into?

A
  • Alpha helices occur when the amino acid sequence folds into a coil / spiral arrangement
  • Beta-pleated sheets occur when the amino acid sequence adopts a directionally-oriented staggered strand conformation

Both α-helices and β-pleated sheets result from hydrogen bonds forming between non-adjacent amine and carboxyl groups

114
Q

What is Proteome?

A

The proteome is the totality of proteins expressed within a cell, tissue or organism at a certain time

115
Q

Discuss and explain the uses of enzymes in industrial processes (8)

A

Enzymes are biological catalyst proteins which speed up the rate of reactions by lowering the amount of activation energy needed for a reaction to begin by providing an alternative pathway. As enzymes lower the amount of activation energy needed, introducing enzymes into an industrial process can allow for lower energy consumption and thus reducing costs. Such an example may be paper production as enzymes assist in the pulping of wood but also the production of biofuel by converting carbohydrates into ethanol which is then used as fuel.. Food production such as beer makes use of enzymes as well as fruit juice production, which relies on pectinase to increase juice yield. The production of lactose free milk is critical for organisms affected by lactose intolerant and relies on the enzyme lactase attached to static beads in order to break down lactose into glucose and galactose, safe for lactose intolerant organisms to consume. Enzymes may also be used for the production of textiles, a popular example is polishing clothes. Another property of enzymes is gene splicing, allowing genetic modification in biotechnology. In medicine the measure of certain enzyme levels in saliva, urine, blood or certain tissues allows us to identify damage or certain diseases in organisms and even pregnancy.

116
Q

Distinguish between DNA and RNA

A

DNA | RNA
Deoxyribose sugar | Ribose sugar
ATGC | AUGC
Double strand | Single strand

117
Q

Outline PCR

A

The polymerase chain reaction (PCR) is an artificial method of replicating DNA under laboratory conditions

The PCR technique is used to amplify large quantities of a specific sequence of DNA from an initial minute sample
Each reaction doubles the amount of DNA – a standard PCR sequence of 30 cycles creates over 1 billion copies (230)

The reaction occurs in a thermal cycler and uses variations in temperature to control the replication process via three steps:

Denaturation – DNA sample is heated (~90ºC) to separate the two strands
Annealing – Sample is cooled (~55ºC) to allow primers to anneal (primers designate sequence to be copied)
Elongation – Sample is heated to the optimal temperature for a heat-tolerant polymerase (Taq) to function (~75ºC)

Taq polymerase is an enzyme isolated from the thermophilic bacterium Thermus aquaticus

As this enzyme’s optimal temperature is ~75ºC, it is able to function at the high temperatures used in PCR without denaturing
Taq polymerase extends the nucleotide chain from the primers – therefore primers are used to select the sequence to be copie

118
Q

Role of lipids in the body

A

Storage of energy for long-term use (e.g. triglycerides)

Hormonal roles (e.g. steroids such as oestrogen and testosterone)

Insulation – both thermal (triglycerides) and electrical (sphingolipids)

Protection of internal organs (e.g. triglycerides and waxes)

Structural components of cells (e.g. phospholipids and cholesterol)

Mnemonic: SHIPS

Biology (13 decks)

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