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Biology > UNIT 1 > Flashcards

UNIT 1 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Monomer (1)

A

• The smaller units from which larger molecules are made

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2
Q

Polymer (1)

A

• Molecules made from a large number of monomers joined together

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3
Q

Monosaccharide (2)

A

• The monomers from which larger
carbohydrates are made

• e.g. glucose, fructose, galactose

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4
Q

Disaccharide (3)

A

• Formed by the condensation of two
monosaccharides

• held together by a glycosidic bond

• e.g. maltose, sucrose, lactose

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5
Q

Polysaccharide (3)

A

• Formed by the condensation of
many glucose units

• held by glycosidic bonds

• e.g. starch, glycogen, cellulose

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6
Q

Cellulose (2)

A

• Polysaccharide in plant cell walls

• formed by the condensation of
β-glucose

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7
Q

Glycogen (2)

A

• Polysaccharide in animals

• formed by the condensation of
α-glucose

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8
Q

Starch (3)

A

• Polysaccharide in plants

• formed by the condensation of
α-glucose

• contains two polymers - amylose
and amylopectin

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9
Q

Glycosidic bond (4)

A

• C–O–C link

• between two sugar molecules

• formed by a condensation reaction

• it is a covalent bond

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10
Q

Amylose (4)

A

• Polysaccharide in starch

• made of α-glucose

• joined by 1,4-glycosidic bonds

• coils to form a helix

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11
Q

Amylopectin (4)

A

• Polysaccharide in starch

• made of α-glucose

• joined by 1,4 and 1,6-glycosidic
bonds

• branched structure

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12
Q

Condensation
reaction (3)

A

• A reaction that joins two molecules
together

• with the formation of a chemical
bond

• involves the elimination of a
molecule of water

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13
Q

Hydrolysis
reaction (3)

A

• A reaction that breaks a chemical
bond

• between two molecules

• involves the use of a water molecule

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14
Q

Fibrils (2)

A

• Long, straight chains of β-glucose
glucose

• held together by many hydrogen
bonds

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15
Q

Triglyceride (2)

A

• Formed by the condensation of one
molecule of glycerol and three
molecules of fatty acids

• forming 3 ester bonds

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16
Q

Phospholipid (3)

A

• Formed by the condensation of one
molecule of glycerol and two
molecules of fatty acid

• held by two ester bonds

• a phosphate group is attached to
the glycerol

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17
Q

Induced-fit
model (4)

A

• The enzyme active site is not
initially complementary to the
substrate

• the active site moulds around the
substrate

• this puts tension on bonds

• lowers the activation energy

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18
Q

Competitive
inhibitor (3)

A

• A molecule that is the same/similar
shape as the substrate

• binds to the active site

• prevents enzyme-substrate
complexes from forming

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19
Q

Non-competitive
inhibitor (3)

A

• A molecule that binds to an enzyme
at the allosteric site

• causing the active site to change
shape

• preventing enzyme-substrate
complexes from forming

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20
Q

Primary
structure (1)

A

• The sequence of amino acids on a
polypeptide chain

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21
Q

Secondary
structure (3)

A

• The folding or coiling

• to create a β pleated sheet or an
α helix

• held in place by hydrogen bonds

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22
Q

Tertiary
structure (3)

A

• The further folding

• to create a unique 3D shape

• held in place by hydrogen, ionic and
sometimes disulfide bonds

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23
Q

Quaternary
structure (1)

A

• More than one polypeptide chain in
a protein

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24
Q

Peptide bond (3)

A

• Covalent bond joining amino acids
together in proteins

• C–N link between two amino acid
molecules

• formed by a condensation reaction

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25
Q

What is the effect of
temperature on enzyme-
controlled reaction (2)

A

• At low temperatures, there is not
enough kinetic energy for
successful collisions between the
enzyme and substrate.

• At too high a temperature,
enzymes denature, the active site
changes shape and enzyme-
substrate complexes cannot form.

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26
Q

What is the effect of pH
on enzyme-controlled
reaction (4)

A

• Too high or too low a pH will
interfere with the charges in the
amino acids in the active site.

• This breaks the ionic and hydrogen
bonds holding the tertiary
structure in place

• therefore the active site changes
shape and the enzyme denatures

• Different enzymes have a different
optimal pH

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27
Q

What is the effect of
substrate concentration
on enzyme-controlled
reaction (3)

A

• At low substrate concentrations,
there will be fewer collisions
between the enzyme and substrate.

• At high substrate concentrations,
the rate plateaus

• because all the enzyme active sites
are saturated

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28
Q

What is the effect of
enzyme concentration
on enzyme-controlled
reaction

A

• At low enzyme concentrations,
there will be fewer collisions
between the enzyme and substrate.

• At high enzyme concentrations, the
rate plateaus

• because there are more enzymes
than the substrate, so many empty
active sites.

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29
Q

Ester bond

A

• –COO– chemical bond

• formed between glycerol and fatty
acids

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30
Q

Hydrophilic

A

• The ability to mix, interact or
attract water

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31
Q

Hydrophobic

A

• The tendency to repel and not mix
with water

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32
Q

Glucose

A

• Monosaccharide that exists as two
isomers

• β glucose and α glucose

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33
Q

Galactose

A

• An example of a monosaccharide
that forms lactose

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34
Q

Fructose

A

• An example of a monosaccharide
that forms sucrose

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35
Q

Isomer

A

• Molecules with the same molecular
formula

• but the atoms are arranged
differently

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36
Q

Maltose

A

• Disaccharide

• formed by the condensation

• of two glucose molecules

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37
Q

Lactose

A

• Disaccharide

• formed by the condensation

• of a glucose molecule and a
galactose molecule

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38
Q

Sucrose

A

• Disaccharide

• formed by the condensation

• of a glucose molecule and a
fructose molecule

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39
Q

Polypeptide

A

• Polymer chain of a protein

• made up of amino acids

• bonded together by peptide bonds

• following condensation reactions

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40
Q

Amino acid

A

• The monomer of a protein

• formed from C,H,O,N

• contains a carboxyl group, amine
group and an R group

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41
Q

Carboxyl group

A

• COOH group

• made up of a C with hydroxyl (OH)
and carbonyl (double-bonded O)
group bonded to it

• found in amino acids and fatty
acids

42
Q

Amine group

A

• NH2 group found on amino acids

43
Q

R group on
amino acids

A

• The variable group

• the part of each of the 20 amino
acids that is different

44
Q

α helix

A

• A secondary structure in proteins

• a coiled shape held in place by
hydrogen bonds

45
Q

β pleated sheet

A

• A secondary structure in proteins

• a folded, pleated shape

• held in place by hydrogen bonds

46
Q

Hydrogen bonds

A

• Weak bond

• forms between H and O

• in many biological molecules e.g.
proteins, water, DNA, tRNA

47
Q

Ionic bonds

A

• A bond that forms between the R
groups of different amino acids

• in the tertiary structure of proteins

48
Q

Disulfide bonds

A

• A strong covalent bond

• between two sulfur atoms in the R
groups of different amino acids

• in the tertiary structure of proteins

49
Q

Active site

A

• Unique-shaped part of an enzyme

• that the substrate binds to

50
Q

Activation energy

A

• The minimum amount of energy
required for a reaction to occur

51
Q

Enzyme-substrate
complex

A

• forms when an enzyme and
substrate collide and bind

• resulting in a lowered activation
energy

52
Q

Denature

A

• When the active site changes shape

• so the substrate can no longer bind

53
Q

Enzyme-inhibitor
complex

A

• The structure that forms when an
enzyme and inhibitor collide and
bind

• prevents enzyme-substrate
complexes from forming

54
Q

Saturated
fatty acid

A

• A long hydrocarbon chain with a
carboxyl group at one end

• only single bonds between carbon
atoms

55
Q

Unsaturated
fatty acid

A

• A long hydrocarbon chain with a
carboxyl group at one end

• at least one double bond between
carbon atoms

56
Q

Polar molecule

A

• A molecule that has an uneven
distribution of charge

57
Q

Phospholipid
bilayer

A

• Phospholipids have two charged
regions

• in water, they are positioned so
that the heads are exposed to
water and the tails are not

58
Q

Plasma
membrane

A

• Phospholipid bilayer

• cell surface membranes and
organelle membranes

59
Q

Reducing sugar

A

• sugars that can reduce Cu ions in
Benedict’s reagent to Cu ions in the
form of copper (I) oxide

• which forms a brick-red precipitate

60
Q

Test for
reducing sugar

A

• Add Benedict’s reagent

• heat

• observe green/yellow/orange/brick
red precipitate

61
Q

How does the structure
of a triglyceride relate
to it’s function?

A

• large ratio of energy-storing
carbon-hydrogen bonds compared
to the number of carbon atoms; a
lot of energy is stored in the
molecule

• high ratio of hydrogen to oxygen
atoms they act as a metabolic
water source

• do not affect water potentials and
osmosis

• have a relatively low mass

62
Q

How does the structure of
a phospholipid relate to
it’s function?

A

• Phospholipids have two charged
regions, so they are polar

• In water, they are positioned so
that the heads are exposed to
water and the tails are not.

• This forms a phospholipid bilayer
which makes up the plasma
membrane around cells.

63
Q

How does the
structure of a
triglyceride and
phospholipid differ?

A

• A phospholipid has one fewer fatty
acid chain

• which is replaced by a phosphate
group

64
Q

What is the difference
between saturated and
unsaturated fatty
acid?

A

• A saturated fatty acid has no
double bonds between carbon
atoms

• where as unsaturated fatty acids
had at least one double bond
between carbon atoms

65
Q

Non-reducing
sugar

A

• a sugar unable to reduce Cu2+

• the glycosidic bond must be
hydrolysed to expose the reducing
group

• e.g. sucrose

66
Q

Test for non-
reducing sugar

A

• Following a negative Benedict’s test

• boil sample in acid and then
neutralise with alkaline

• add Benedict’s reagent and heat

• observe orange/brick red colour

67
Q

Test for starch

A

• Add iodine

• turns blue/black

68
Q

Test for lipids

A

• Add ethanol and shake
to dissolve

• then add water

• white emulsion forms

69
Q

Test for protein

A

• Add biuret

• turns purple

70
Q

Nucleotide

A

• The monomer of DNA and RNA

• contains a pentose sugar, a
phosphate group and a nitrogenous
base

71
Q

Nitrogenous
base

A

• Part of a nucleotide

• adenine, guanine, cytosine, thymine
and uracil

72
Q

DNA nucleotide

A

• The monomer of DNA

• contains a deoxyribose sugar, a
phosphate group and a nitrogenous
base

73
Q

Polynucleotide

A

• DNA polymer

• many nucleotides
joined together via
a condensation
reaction

• joined by
phosphodiester
bonds

74
Q

Phosphodiester
bond

A

• Bond joining two nucleotides
together

• forms between a phosphate group
and the pentose sugar

75
Q

Complementary
base pairs

A

• The base pairs that align opposite
each other and form hydrogen
bonds

• adenine and thymine/uracil

• guanine and cytosine

76
Q

Ribose

A

• pentose sugar

• found in RNA nucleotide and ATP

77
Q

Uracil

A

• Nitrogenous base
• found in RNA instead of thymine

78
Q

mRNA

A

• a copy of a gene

• single-strand polymer of RNA

79
Q

tRNA

A

• found only in the cytoplasm

• single-stranded but folded to
create a shape that looks like a
cloverleaf

• held in place by hydrogen bonds

80
Q

rRNA

A

• rRNA combines with protein to
make ribosomes

81
Q

DNA template
strand

A

• A DNA strand that is used to make a
new DNA copy from

• both DNA strands in the double
helix are used as templates in DNA
replication

82
Q

DNA polymerase

A

• An enzyme in DNA replication

• joins together adjacent nucleotides

83
Q

Semi-conservative
replication

A

• DNA replication is semi-
conservative replication

• one strand is from the parental
DNA and one strand is newly
synthesised

84
Q

DNA helicase

A

• Enzyme that breaks hydrogen
bonds between the two chains of
DNA in a double helix

• causes the two strands to separate

• involved in DNA replication and
transcription

85
Q

Large latent heat
of vaporisation

A

• a lot of energy is required to convert
water from its liquid state to a
gaseous state

• this is due to the hydrogen bonds,
as energy is needed to break these
to turn it into a gas

• means water can provide a cooling
effect

86
Q

High specific
heat capacity

A

• a lot of energy is required to raise
the temperature of the water

• because some of the heat energy is
used to break the hydrogen bonds
between water molecules

• important so water can act as a
temperature buffer

87
Q

Metabolite

A

• Water is involved in many reactions

• such as photosynthesis, hydrolysis,
and condensation reactions

88
Q

Solvent

A

• Water is a good solvent

• meaning many substances dissolve
in it

• polar (charged) molecules dissolve
readily in water due to the fact
water is polar

89
Q

Strong
cohesion

A

• water molecules ‘stick’ together
due to hydrogen bonds

• results in water moving up the
xylem as a continuous column of
water

• provides surface tension, creating
a habitat on the surface of the
water for small invertebrates

90
Q

ATP synthase

A

• Enzyme that catalyses the
synthesis of ATP from ADP + Pi

91
Q

ATP hydrolase

A

• Enzyme that catalyses the
hydrolysis of ATP into ADP +Pi

92
Q

Phosphorylation

A

• The addition of a phosphate group
to a molecule

• making the molecule more
reactive/it gains energy

93
Q

Structure of
water

A

• Water is a polar molecule

• the oxygen atom is slightly
negative

• the hydrogen atoms are slightly
positive

94
Q

Dipeptide

A

• Two amino acids bonded together
by a peptide bond

• formed by a condensation reaction

95
Q

RNA nucleotide

A

• monomer of RNA

• composed of a phosphate group,
ribose and a nitrogenous base

• has the base uracil instead of
thymine

96
Q

Role of
hydrogen ions

A

• determine the pH

• the more hydrogen ions, the more
acidic the conditions are

• an important role in chemiosmosis
in respiration and photosynthesis

97
Q

Role of
iron ions

A

• a compound of haemoglobin

• involved in oxygen transport

98
Q

Role of sodium ions
in co-transport

A

• involved in co-transport for
absorption of glucose and amino
acids in the ileum

99
Q

Role of
phosphate ions

A

• as a component of DNA, RNA and
ATP

• phosphodiester bond in DNA and
RNA forms between the phosphate
group and the pentose sugar

100
Q

Fatty acid
structure

A

• carboxyl group and a long
hydrocarbon chain

• can be saturated or unsaturated

Biology (3 decks)

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