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bio moles (1) Flashcards

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Biology 101 flashcards
1
Q

what is the formula of glucose

A

C6H1206

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2
Q

what do alpha and beta glucose have in common

A

they are both 6-carbon hexose sugars

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3
Q

how is the structure of glucose adapted to its function

A

they are small + water soluble -> meaning they are easily transported in the blood

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4
Q

what are the 3 monosaccharides

A

glucose fructose galactose

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5
Q

what are the 3 disaccharides

A

maltose sucrose lactose

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6
Q

what is maltose made of

A

2 glucose

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7
Q

what is sucrose made of

A

glucose + fructose

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8
Q

what is lactose made of

A

glucose + galactose

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9
Q

what are the bonds between monosaccharides

A

glycosidic

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10
Q

how are glycosidic bonds formed

A

condensation reactions

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11
Q

what are the 3 polysaccharides

A

starch glycogen cellulose

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12
Q

describe the structure of starch

A

make up of amylose + amylopectin

amylose
- 1,4 bonds
- helix with intermolecular H bonds -> making it compact

amylopectin
- 1,4 and 1,6 bonds
- highly branched -> meaning many terminal ends for hydrolysis into glucose

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13
Q

give 2 structural benefits of starch

A

large -> meaning it doesn’t diffuse out of cells

insoluble -> meaning no osmotic effect on cells

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14
Q

what is the function of starch

A

for storage of a-glucose in plants

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15
Q

describe the structure of glycogen

A
  • made up of a-glucose
  • 1,4 and 1,6 bonds
  • highly branched -> meaning many terminal ends for hydrolysis into glucose
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16
Q

give 2 structural benefits of glycogen

A

large -> meaning it doesn’t diffuse out of cells

insoluble -> meaning no osmotic effect on cells

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17
Q

what is the function of glycogen

A

for storage of a-glucose in animals and fungi

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18
Q

describe the structure of cellulose

A
  • made up of b-glucose
  • 1,4 bonds
  • unbranched + straight chained
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19
Q

give a structural benefit of cellulose

A

H-bonds between parallel strands form microfibrils -> which gives it a high tensile strength

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20
Q

what is the function of cellulose

A

it gives rigidity to plant cell walls

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21
Q

what is the structure of a triglyceride

A

1 glycerol + 3 fatty acids

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22
Q

what are the bonds in triglycerides

A

ester bonds

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23
Q

how are ester bonds formed

A

condensation reactions

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24
Q

contrast the structure of saturated and unsaturated fatty acids

and state where they are found

A
  • saturated only have single bonds between carbons whereas unsaturated also has double
  • saturated are straight chained molecules with many contact points
    whereas unsaturated are kinked molecules with fewer contact points
  • saturated have a higher melting point and are solid at room temp
    whereas unsaturated have a lower melting point and are liquid at room temp
  • saturated are found in animal fats whereas unsaturated are found in plant oils
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25
Q

state how the structure of triglycerides relates to their role

A

high energy:mass radio -> meaning high energy storage (double calories/gram than carbs)

insoluble hydrocarbon chain -> means there is no effect on the osmotic potential of cells + can be used for waterproofing

its a slow conductor of heat -> useful for thermal insulation

its less dense than water -> giving buoyancy to aquatic animals

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26
Q

what is the structure phospholipids

A

a glycerol backbone attached to 1 hydrophilic polar phosphate head + 2 hydrophobic fatty acid tails

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27
Q

state how the structure of phospholipids relates to their role

A

its amphipathic (has both hydrophobic and hydrophilic parts) -> so it forms the phospholipid bilayer of cell membranes

its tails can splay outwards -> waterproofing

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28
Q

how many R groups are there

A

20

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29
Q

what are the bonds between amino acids

A

peptide bonds

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30
Q

how are peptide bonds formed

A

condensation reactions

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31
Q

describe the primary structure of a protein

A

the sequence of amino acids in a polypeptide chain

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32
Q

describe the secondary structure of a protein

A

folding of the polypeptide chain into an alpha helix or beta pleated sheet

hydrogen bonds added

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33
Q

describe the tertiary structure of a protein

A

the further folding of the polypeptide into a 3D structure

ionic and disulphide bridges are added

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34
Q

describe the quaternary structure of a protein

A

this is the final arrangement of several polypeptides
it can either be globular or fibrous

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35
Q

what are the ionic bonds doing

A

forming between oppositely charged R groups

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36
Q

what are the disulphide bridges doing

A

they are covalent bonds between sulphur

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37
Q

describe the structure and function of globular proteins

A
  • soluble
  • (sometimes) have a complex quaternary structure
  • used in metabolic processes
  • e.g. haemoglobin, enzymes, antibodies
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38
Q

describe the structure and function of fibrous proteins

A
  • insoluble
  • mainly secondary structure
  • used for structure + support
  • e.g. collagen
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39
Q

describe the structure of haemoglobin

A

4 polypeptides
each has 1 haem group
contains Fe2+ ions
oxygen binds to Fe2+
oxygen carried in blood
and released when required
e.g. in tissues for respiration

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40
Q

describe the structure of collagen

A

triple helix made of 3 polypeptides
many H and disulphide bonds
gives it a high tensile strength
used as a component in bones, cartilage and connective tissue

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41
Q

what is the structure of a nucleotide

A

pentose sugar, nitrogenous base + a phosphate group

42
Q

what are the bonds between nucleotides

A

phosphodiester bonds

43
Q

how are phosphodiester ester bonds formed

A

condensation reactions

44
Q

describe the structure of DNA

A

double helix

2 sugar phosphate backbones joined together by hydrogen bonds between complementary bases

sugar phosphate backbones are polynucleotides

45
Q

name the purines

A

A + G

2-ring molecules

46
Q

name the pyrimidines

A

C+ T (and U)

1-ring molecules

47
Q

what is semi-conservative replication

A

a strand from the original DNA molecule acts as a template

the new DNA molecule contains 1 old + 1 new strand

48
Q

name the enzymes involved in semi-conservative replication

A

helicase, polymerase + ligase

49
Q

explain the role of DNA helicase

A

helicase breaks the H-bonds between base pairs via

forming 2 single strands with exposed bases

which act as a template

50
Q

explain the role of DNA polymerase

A

polymerase joins adjacent nucleotides onto the new strand
in a 5’ -> 3’ direction
via condensation reactions
forming phosphodiester bonds

H-bonds then reform between complementary bases

51
Q

explain the role of DNA ligase

A

ligase joins gaps in fragments
to form a continuous strand

52
Q

what is a gene

A

a sequence of bases on a DNA molecule
coding for a specific sequence of amino acids in a polypeptide chain

53
Q

what is the genome

A

all of the DNA in an organism

54
Q

describe the structure of mRNA

A

1 sense strand
composed of a sugar phosphate backbones + codons

55
Q

describe the structure of tRNA

A

an anticodon (3 bases)

56
Q

name the stages of protein synthesis

A
  1. translation
  2. splicing
  3. translation
57
Q

what is transcription

A

making mRNA from a strand of DNA in the nucleus

58
Q

explain the process of transcription

A

DNA polymerase binds onto DNA at certain sites
a small part of the DNA uncoils into 2 strands with exposed bases

free nucleotides attach to antisense strand

RNA polymerase joins adjacent nucleotides by phosphodiester bonds

59
Q

what happens between transcription and translation

A
  1. splicing (only in eukaryotes)
    introns are removed
    turning pre mRNA to mRNA
  2. the mRNA then moves out of the nucleus via a nuclear pore and to the ribosomes
60
Q

what is translation

A

making proteins from mRNA in ribosomes (found in the cytoplasm or on the rough ER)

61
Q

explain the process of translation

A

mRNA attaches to a ribosome

tRNA anticodon attaches to codon on mRNA
ribosome catalyse condensation reactions between animo acids on tRNA
forming peptide bonds

process continues
until stop codon is reached on mRNA
then the polypeptide + mRNA is released

62
Q

what is the role of ATP in translation

A

the hydrolysis of ATP provides energy to form peptide bonds between amino acids

63
Q

state 2 characteristics of the genetic code

A

it is non-overlapping -> meaning each triplet is only read once

it is degenerative -> meaning many triplets code for the same amino acid (64 possible triplets for only 20 amino acids)

64
Q

what is a DNA triplet

A

a sequence of 3 bases that codes for a particular amino acid

65
Q

what is a start codon

A

a triplet on mRNA that initiates the translation of the polypeptide

66
Q

what is a stop codon

A

a triplet on mRNA that terminates translation of the polypeptide

67
Q

what are exons

A

coding regions of DNA

68
Q

what are introns

A

non-coding regions of DNA

69
Q

what is a gene mutation

A

any change in the base sequence of DNA
often arises spontaneously during replication

70
Q

what can increase the risk of mutations

A

mutagens e.g. chemicals, radiation

71
Q

name the types of mutations

A

substitution, deletion, insertion + point

72
Q

explain a substitution mutation

A

a base from each strand is replaced with another

(if the new codon codes for the same amino acid)
it is likely to be silent
causing no change to the amino acid sequence

73
Q

explain a deletion mutation

A

a base is lost from each strand
causing a frame shift
entire sequence past the point of the mutation will be different

meaning the mutation is likely to be significant

74
Q

explain a insertion mutation

A

one or more bases is added to each strand
causing frame shift
entire sequence past the point of the mutation will be different

meaning the mutation is likely to be significant

75
Q

explain the causes and effects of sickle cell anaemia

A

caused by a substitution in the gene that codes for haemoglobin

change in the primary structure
meaning a different tertiary
resulting in abnormal haemoglobin molecules
makes RBCs sickle shaped
impairing their ability to transport oxygen
causing a rapid heartbeat, fatigue + dizziness

RBCs can also get stuck in vessels
this is called sickle crisis
causing tissue damage + severe pain

76
Q

describe the structure of enzymes

A

globular proteins

tertiary structure determines shape of active site
complementary to a specific substrate

77
Q

explain the function of enzymes

A

act as biological catalysts

the formation of enzyme-substrate complexes
lowers the activation energy
of metabolic reactions

78
Q

explain the induced fit model

A

a theory that suggests the shape of enzymes active site is NOT directly complementary to the substrate

instead
conformation change (a change in tertiary structure as a response to external factors e.g. temp, pH)
enables enzyme-substrate complexes to form
this puts strain on substrate bonds
lowering activation energy

79
Q

name the factors affecting enzyme controlled reactions

A

temperature, pH, enzyme conc, substrate conc

80
Q

how does temperature effect enzyme reactions

A

as temperature increases
kinetic energy increases
rate of reaction increases

above optimum
H + ionic bonds in tertiary structure break
denaturing the active site

81
Q

how does pH effect enzyme reactions

A

narrow optimum pH range

outside ranges
(H+ if too acidic or hydroxide if too alkaline) interact with H + ionic bonds in tertiary structure
denaturing the active site

82
Q

how does enzyme concentration effect enzyme reactions

ADJUST

A

when substrate is in excess
the rate increases proportionally to the enzyme conc
max number of complexes forming at a given time= rate levels off

83
Q

how does substrate concentration effect enzyme reactions

ADJUST

A

when enzyme is in excess
the rate increases proportion to the substrate conc

84
Q

what are the types of inhibitors

A

competitive, non-competitive + end-product

85
Q

what are competitive inhibitors

A

they have a similar shape as the substrate
therefore bind to active sites
temporarily preventing enzyme-substrate complexes from forming
until released

increasing substrate conc = decreases their effect

86
Q

what are non-competitive inhibitors

A

they bind at the allosteric binding sites
triggering conformational change of actives sites

increasing substrate conc = no impact on their effect

87
Q

what is end-product inhibition

A

when the product of a reaction acts as a competitive or non-competitive inhibitor for an enzyme involved in the pathway
preventing further formation of the products

88
Q

how do you calculate the rate of enzyme activity from a graph

A

use the initial rate
so the gradient at 0s

89
Q

why do we calculate the initial rate of a reaction

A

its the only point where the concentration of both enzymes and substrates is known
allowing for comparisons

neither are limiting factors affecting the rate yet

90
Q

name the ions found in plants

A

nitrate, calcium, magnesium + phosphate

91
Q

describe the role of nitrate ions

A

to make amino acids and DNA

92
Q

describe the role of calcium ions

A

to make calcium pectate for the middle lamellae

93
Q

describe the role of magnesium ions

A

to make chlorophyll

94
Q

describe the role of phosphate ions

A

to make ATP and ADP

95
Q

explain what is meant by the dipole nature of water

A

O is more electronegative
so it attracts more electrons in the covalent bond

H bonds form between other dipolar water molecules

96
Q

state the 5 important properties of water

A

high specific heat capacity
polar solvant
high surface tension
incompressibility
maximum density at 4C

97
Q

what is the importance of water having a high specific heat capacity

A

it acts as a temperature buffer
enabling endotherms to resist fluctuations in their body temperature
maintaining optimum enzyme activity

98
Q

what is the importance of water being a polar solvent

A

means it is able to dissolve and transport ions in bodily reactions

99
Q

what is the importance of water having a high surface tension

A

slows water loss via transpiration in plants

water rises unusually high in narrow tubes
lowering demand on root pressure

provides a habitat for insects who can skim across the surface of water

100
Q

what is the importance of water being incompressible

A

it provides turgidity to plant cells

it provides a hydrostatic skeleton for some small organisms e.g. earthworm

101
Q

what is the importance of water having a maximum density at 4C

A

ice is less dense than water
causing it to float
insulating water underneath in cold climates
allowing aquatic organisms to survive

bio (4 decks)

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