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Biology > Module 1 - Biological Molecules > Flashcards

Module 1 - Biological Molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

whats a monomer

A

a small, single-molecule, many of which can be joined together to form a polymer

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2
Q

whats a polymer

A

a large molecule made up of many identical/similar monomers joined together

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3
Q

whats a condensation reaction

A

joins 2 molecules together, eliminates a water molecule, and forms a chemical bond

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4
Q

whats a hydrolysis reaction

A

separates 2 molecules, requires the addition of water molecule, and breaks a chemical bond

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5
Q

whats a monosaccharide

A

monomers from which larger carbohydrates are made

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6
Q

whats disaccharide

A

condensation of 2 monosaccharides

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7
Q

whats a polysaccharide

A

condensation of many monosaccharides

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8
Q

give 3 examples of monosaccharides

A

glucose, fructose, and galactose

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9
Q

how do you make maltose

A

glucose + glucose

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10
Q

how do you make sucrose

A

glucose + fructose

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11
Q

how do you make lactose

A

glucose + galactose

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12
Q

whats the bond between disaccharides

A

glycosidic

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13
Q

what are the two isomers of glucose

A

alpha and beta

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14
Q

draw alpha and beta glucose

A

refer to notes

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15
Q

give 3 examples of polysaccharides

A

starch, glycogen, and cellulose

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16
Q

whats glycogens function

A

energy store in animal cells

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17
Q

what’s the structure of glycogen

A

the polysaccharide of alpha glucose with alpha 1,4 and 1,6 glycosidic bonds

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18
Q

relate 3 properties of glycogen to its function

A

branched - rapidly hydrolyzed to release glucose and provide energy for respiration
large molecule - can’t leave the cell
insoluble in water - water potential of cell not effected

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19
Q

whats starches function

A

energy store in plant cells

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20
Q

whats starches structure

A

the polysaccharide of alpha glucose - a mix of amylose and amylopectin

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21
Q

structure of amylose

A

alpha 1,4 glycosidic bonds so unbranched

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22
Q

structure of amylopectin

A

alpha 1,4 and 1,6 glycosidic bonds so branched

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23
Q

relate 3 properties of starch (amylose) to its function

A

helical - compact for storage in the cell
large molecule - can’t leave the cell
insoluble in water - water potential of cell not effected

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24
Q

what’s the function of cellulose

A

provides strength and structural support to plant cell walls

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25
Q

relate 4 properties of starch (cellulose) to its function

A

every other beta glucose molecule is inverted in a long, straight, unbranched chain
many hydrogen bonds - link parallel strands to form microfibrils
hydrogen bonds strong in high numbers - provides strength and structural support to plant cell walls

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26
Q

give examples of reducing sugars

A

all monosaccharides and maltose/lactose

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27
Q

give examples of non-reducing sugars

A

no monosaccharides and sucrose

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28
Q

what the benedicts test used for

A

reducing sugar

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29
Q

how to perform the benedicts test

A

add benedicts reagent to sample, heat in a boiling water bath

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30
Q

whats the positive result for the benedicts test

A

blue to red precipitate

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31
Q

how to test for non-reducing sugars

A

add few drops of dilute HCl, heat in boiling water bath, neutralize with NaHCO3, add benedicts reagent, and heat again

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32
Q

whats the positive result for the non-reducing sugars test

A

blue to red precipitate

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33
Q

how to perform a starch test

A

add iodine dissolved in potassium iodide to solution and shake

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34
Q

whats the positive test result for the starch test

A

blue-black color

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35
Q

how to determine glucose concentration

A
  1. Produce a dilution series of glucose solutions of known concentrations
  2. Perform Benedict’s test on each sample
    • Heat with Benedict’s solution
    • Use the same amount of solution for each test
    • Use excess Benedict’s
    • Remove precipitate by filtering
  3. Using a colorimeter, measure the absorbance of each sample and plot a calibration curve
    • Calibrate colorimeter using unreacted Benedict’s
    • Use a red filter
    • Less absorbance of filtrate = more sugar present (as removed precipitate)
    • Plot absorbance against glucose concentration
  4. Repeat with unknown sample (find absorbance) and use the graph to determine glucose concentration
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36
Q

what are the 2 types of lipid

A

triglycerides and phospholipids

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37
Q

whats a triglyceride

A

the condensation reaction between 1 molecule of glycerol and 3 fatty acids

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38
Q

what’s the bond in lipids

A

ester bonds

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39
Q

relate 2 properties of triglycerides to their structure

A

high ratio of C-H bonds to C atoms in hydrocarbon tail so release more energy than the same mass of carbohydrates
Insoluble - no effect on water potential of cell

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40
Q

how is an ester bond formed

A

the condensation reaction between glycerol and fatty acid (RCOOH)

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41
Q

whats a phospholipid

A

the condensation reaction between 1 molecule of glycerol, 2 fatty acids, and a phosphate group

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42
Q

what do phospholipids do

A

form bilayer in the cell membrane - allows diffusion of small/ non-polar molecules

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43
Q

relate 2 properties of phospholipids to their structure

A

phosphate heads are polar/hydrophilic so are attracted to water so face the aqueous environment on either side of the membrane
fatty acid tails are non-polar/hydrophobic so are repelled by water so face inside of the membrane and repel polar/charged molecules

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44
Q

what’s meant by saturated fatty acid

A

no C=C double bonds in the hydrocarbon chain

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45
Q

what’s meant by unsaturated fatty acid

A

one or more C=C double bonds in the hydrocarbon chain

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46
Q

what the emulsion test for lipids

A

add ethanol and shake

then add water

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47
Q

what the positive result for the emulsion test for lipids

A

milky white emulsion

48
Q

whats an amino acid

A

the monomers from which proteins are made

49
Q

whats the bond between 2 or more amino acids

A

peptide bond

50
Q

what are the different groups of an amino acid

A

NH2 - amino group
COOH - carboxyl group
R group - side group –> produces 20 different amino acids

51
Q

draw the amino acid general structure

A

refer to notes

52
Q

whats a dipeptide

A

the condensation reaction between 2 amino acids to form a peptide bond

53
Q

whats a polypeptide

A

the condensation reaction between many amino acids to form a peptide bond

54
Q

silly little fact

A

a functional protein may contain one or more polypeptides

55
Q

whats the primary structure of a protein

A

the sequence of amino acids in a polypeptide chain

56
Q

whats the secondary structure of a protein

A

hydrogen bonding between amino acids (between carbonyl O of one and amino H of another)
causes polypeptide chain to fold into a repeating patter - alpha helix or beta plated sheets

57
Q

whats the tertiary structure of a protein

A

overall 3d structure of a polypeptide held together by interactions between amino acids and side chains - ionic bonds, disulphide bridges and hydrogen bonds

58
Q

whats the quarternary structure of a protein

A

some proteins made up of 2+ polypeptide chains

held together by more hydrogen, ionic, and disulfide bridges

59
Q

what the test for proteins

A

biuret test

60
Q

how to perform the biuret test

A

add biuret solution - NaOH + CuSO4

61
Q

what the results of the biuret test

A

positive=purple colour

negative=stays blue

62
Q

what are enzymes

A

a biological catalyst that lowers the activation of the reaction it catalyzes so speeds up the rate of reaction

63
Q

what reactions do enzymes catalyze

A

intracellular and extracellular

64
Q

what the induced fit model

A

before reaction = enzymes active site isn’t complementary to the substrate
active site changes shape as substrate binds and E-S complex forms
this distorts bonds in substrate leading to reaction

65
Q

outline the specificity of enzymes

A

. have a specific shaped tertiary structure and active site and primary structure determine the tertiary structure
. active site complementary to a specific substrate
.only specific substrate can bind to active site, forms E-S complex

66
Q

how does enzyme concentration affect ROR

A

Increasing enzyme conc = ROR increases
Enzyme conc = limiting factor (substrate in excess)
More enzymes more available active sites
More successful E-S collisions and E-S complex

At a certain point, rate of reaction plateaus
Substrate conc. = limiting factor (all substrates in use)

67
Q

how does substrate concentration affect ROR

A

increasing substrate conc=rate of reaction increases
Substrate concentration = limiting factor (too few
enzyme molecules to occupy all active sites)
More successful E-S collisions and E-S complexes

At a certain point, rate of reaction plateaus
Enzyme conc. = limiting factor (all active sites
saturated; excess substrate)

68
Q

how does increasing temp to optimum effect ROR

A

Increasing temp up to optimum= rate of reaction increases
Increase in kinetic energy
More successful E-S collisions and E-S complexes

69
Q

how does increasing temp past optimum effect ROR

A

Increasing temp. above optimum=rate of reaction falls
Enzymes denature; tertiary structure and active site
change shape (hydrogen / ionic bonds break)
Fewer E-S collisions and E-S complexes (substrate no
longer binds to active site)
Rate of reaction 0 when all enzymes denatured

70
Q

how does increasing pH above/below optimum effect ROR

A

rate of reaction decreases
Enzymes denature; tertiary structure and active site change shape (hydrogen and ionic bonds break)
The complementary substrate can no longer bind to active site
Fewer E-S collisions and E-S complexes

71
Q

how to calculate pH

A

pH = - log10 [H+]

72
Q

how do competitive inhibitors decrease ROR

A

similar shape to the substrate
binds and blocks active site so substrate cant bind
fewer E-S complexes form

73
Q

how to combat the effect of competitive inhibitors

A

increase substrate concentration

74
Q

how do non-competitive inhibitors decrease ROR

A

binds to the allosteric site
enzymes tertiary structure changes so active site changes shape so substrate cant bind
fewer E-S complexes form

75
Q

how to combat the effect of non-competitive inhibitors

A

you cant - increasing substrate concentration has no effect as permanent damage done to the active site

76
Q

whats the function of DNA

A

holds genetic information

77
Q

whats the function of RNA

A

transfer genetic information from DNA to ribosomes

78
Q

what are ribosomes made from

A

RNA and proteins

79
Q

what the structure of a nucleotide

A

pentose sugar, a nitrogenous base, and a phosphate group

80
Q

what bonds formed between nucleotides after a condensation reaction

A

phosphodiester bonds

81
Q

whats DNA

A

2 antiparallel strands, held together by hydrogen bonds between specific complementary base pairs (A-T and C-G) twisting into a double helix

82
Q

whats RNA

A

single RNA polynucleotide strand

83
Q

give two differences between DNA and RNA nucleotides

A

DNA nucleotides have a deoxyribose sugar whereas RNA has a ribose pentose sugar
DNA nucleotides have the thymine base whereas RNA nucleotides have uracil

84
Q

give two differences between DNA and RNA molecules

A

DNA is double-stranded whereas RNA is single stranded

DNA is longer whereas RNA is shorter

85
Q

relate 7 DNA structure components to its function

A 
Double-stranded = both strands can act as a template in semi-conservative DNA replication
Weak hydrogen bonds between bases = unzipped for replication
Complementary base pairing = accurate replication
Many hydrogen bonds between bases = stable/strong molecule
Double helix with sugar-phosphate backbone = protects bases
Long molecule = store lots of genetic information
Double helix (coiled) = compact
86
Q

how to use incomplete information about the frequency of bases on DNA strands to find the frequency of other bases

A

% of adenine in strand 1 = % of thymine in strand 2 (and vice versa)
% of guanine in strand 1 = % of cytosine in strand 2 (and vice versa)

87
Q

outline process of semi-conservative DNA replication

A
  1. DNA Helicase breaks hydrogen bonds between bases, unwinds the double helix
  2. Two strands which both act as templates
  3. Free-floating DNA nucleotides attracted to exposed bases via specific complementary base
    pairing, hydrogen bonds form (adenine-guanine; guanine-cytosine)
  4. DNA polymerase joins adjacent nucleotides on a new strand by condensation, forming phosphodiester bonds
  5. Replication is semi-conservative – each new strand formed contains one original template strand
    and one new strand
  6. Ensures genetic continuity between generations of cells
88
Q

why does DNA polymerase move in opposite directions along the DNA strands

A

DNA has antiparallel strands
DNA polymerase is an enzyme with a specific shaped active site that can only bind to substrate with
a complementary shape
Can only bind to and add nucleotides to the phosphate (3’) end of the developing strand (so works in a
5’ to 3’ direction)

89
Q

whats the evidence for semi-conservative replication

A

Meselson and Stahl

90
Q

what is involved in the Meselson and Stahl experiment

A

Bacteria were grown in a nutrient solution containing heavy nitrogen (15N)
for several generations
• Nitrogen incorporated into bacterial DNA bases
• Bacteria then transferred to a nutrient solution containing light
nitrogen (14N) and allowed to grow and divide twice
• During this process, DNA from different samples of bacteria was
extracted, suspended in a solution in separate tubes and spun in a
centrifuge

91
Q

whats the results of the Meselson and Stahl experiment

A

Sample 1 = DNA from bacteria grown for several generations in a nutrient solution containing 15N
DNA molecules contain 2 ‘heavy’ strands

Sample 2 = DNA from bacteria grown originally in a nutrient solution containing 15N, then transferred for one division to a solution containing 14N so DNA molecules contain 1 original ‘heavy’ and 1 new ‘light strand

Sample 3 = DNA from bacteria grown originally in a nutrient solution 15N, then transferred for two divisions to a solution containing 14N 50% DNA molecules contain 1 original ‘heavy’ and 1 new ‘light’ strand, 50% contain both ‘light’ strands

92
Q

whats the structure of ATP

A

a ribose sugar, a molecule of adenine and, 3 phosphate groups

93
Q

whats the structure of ADP

A

a ribose sugar, a molecule of adenine and, 2 phosphate groups

94
Q

what is ATP

A

a nucleotide derivative

95
Q

outline the process of hydrolysis of ATP

A

ATP is hydrolyzed into ADP and Pi and is catalyzed by ATP hydrolase and energy released when bonds between inorganic phosphate groups are broken
The inorganic phosphate released can be used to
phosphorylate other compounds -making them more reactive

96
Q

outline the process of formation of ATP

A

ADP and Pi undergo a condensation reaction which is catalyzed by the ATP synthase
Happens during respiration
Called phosphorylation of ADP

97
Q

what are the properties of ATP that make it a suitable immediate source of energy

A

ATP releases energy in small, manageable amounts so no energy wasted
Only one bond is hydrolyzed to release energy which is why energy release is immediate

98
Q

Can ATP be stored

A

no

99
Q

how does hydrogen bonding occur between water molecules

A

Water is a polar molecule so slightly negatively charged oxygen atoms attract slightly positively charged hydrogen atoms of other water molecules so hydrogen bonds form between water molecules

100
Q

what are the 5 properties of water that is important in biology

A

high specific heat capacity, high latent heat of vaporization, cohesive, solvent, and metabolite

101
Q

explain the property of high specific heat capacity

A

Polar so many H bonds form between water molecules
these allow water to absorb a relatively large amount of
heat energy before its temperature changes

102
Q

explain the property of high latent heat of vaporization

A

Polar so many H bonds form between water molecules
these can absorb a lot of energy before breaking,
when water evaporates

103
Q

explain the property of cohesive

A

Polar so many H bonds form between water molecules

so water molecules tend to stick together

104
Q

explain the property of solvent

A 
Polar (has slightly positive and negative ends)
Can separate (dissolve) ionic compounds e.g. NaCl as +ve end attracted to -ve ion (Cl-) and negative end attracted to positive ion (Na+)
105
Q

explain the property of metabolite

A

Water is reactive

106
Q

whats the importance of high specific heat capacity in biology

A

Good habitat for aquatic organisms e.g. lakes as
temperature more stable than land
Organisms mostly made of water so helps maintain
a constant internal body temperature – important
as temperature affects enzyme activity

107
Q

whats the importance of high latent heat of vaporization in biology

A

Evaporation of small amount of water (e.g. sweat)
is an efficient cooling mechanism
• Helping organisms maintain a constant body
temperature

108
Q

whats the importance of cohesion in biology

A

Column of water doesn’t break when pulled up a
narrow tube e.g. xylem during transpiration
• Produces surface tension at an air-water surface so
invertebrates can walk on water e.g. pond skaters

109
Q

whats the importance of solvent in biology

A

Can dissolve other substances e.g. inorganic ions,
enzymes, urea, etc. so water…
• Acts as a medium for metabolic reactions (which
can happen in water)
• Acts as a transport medium e.g. in xylem to
transport nitrates which are needed to make
amino acids

110
Q

whats the importance of metabolite in biology

A

Condensation releases H2O and forms a chemical
bond; hydrolysis requires H2O to break a bond; e.g.
amino acids joined by condensation reactions to
form polypeptides

111
Q

where and how do inorganic ions occur

A

Occur in solution in the cytoplasm and body fluids of organisms, some in high concentrations and others in very low concentrations

112
Q

name the 4 inorganic ions

A

phosphate, hydrogen, iron and, sodium

113
Q

what the role of phosphate

A

Attached to other molecules as a phosphate group such as in DNA nucleotides enabling nucleotides to join together forming phosphodiester bonds and in ATP as bonds between these store/release energy

114
Q

what the role of hydrogen

A

Maintain pH levels in the body
• Too much H+ = acidic (low pH)
• Too little H+ = alkaline (high pH)
• Affects rate of enzyme-controlled reactions as can cause enzymes to denature

115
Q

what the role of iron

A 
Component of (haem group of) haemoglobin which is contained in red blood cells that transports oxygen around the body – oxygen temporarily binds to it, so it
becomes Fe3+
116
Q

what the role of sodium

A

Co transport of glucose and amino acids across cell membranes
Involved in generating nerve impulses and muscle contraction

Biology (3 decks)

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