2.1.3 nucleic acids and 2.1.4 Enzymes Flashcards

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1
Q

Biological catalysts

A

catalysts in living organisms
work at lower temp and pressure to chemical catalysts
speeds up reaction without being used up

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2
Q

what type of protein are enzymes

A

globular
specific shape
water soluble

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3
Q

what do enzymes do to the activation energy of a reaction

A

decrease it
less energy needed to start a reaction
provide alternative pathway by holding reacting groupps close together or put strain on the bonds

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4
Q

Anabolic reactions

A

enzymes make large molecules out of smaller ones

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5
Q

Catabolic reactions

A

break large molecules into smaller ones

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6
Q

metabolism

A

sum total of all reactions happening in cell or organism

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7
Q

metabollic pathway

A

essential process for life

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8
Q

Intracellular enzymes

A

enzymes produced and act inside the same cell

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9
Q

extracellular enzymes

A

enzymes act outside the cell in which they were produced

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10
Q

why is extracellular enzymes neccessary

A

large molecules cant fit into the cell directly through the plasma membrane

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11
Q

example of intracellular enzyme

A

catalase
ensure hydrogen peroxide is broken down to oxygen and water

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12
Q

example of extracellular enzyme

A

digestion
break large molecules into smaller ones

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13
Q

Amylase

A

produced by salivary glands and pancreas
released into saliva and pancreatic juice
breaks down starch polymers into maltose

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14
Q

trypsin

A

a protease
digestion of proteins into smaller peptides which can be further broken down into amino acids

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15
Q

lock and key hypothesis

A

substrate fits into active sit of only one enzyme
when substrate binds it forms enzyme substrate complex
products are produced and released

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16
Q

induced fit hypothesis

A

substrate cause enzyme to change shape slightly as it binds
shape of active site is NOT fixed

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17
Q

Active site

A

made of 6-10 amino acids

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18
Q

precursor activation

A

the activation of an inactive enzyme

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19
Q

how can enzymes be activated

A

change to their tertiary structure
change in their enviroment
addition of a non protein helper (cofactor)

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20
Q

cofactors

A

non protein molecule that binds to an enzyme to activate it
An enzyme that needs one can’t function without it

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21
Q

3 types of cofactors

A

prosthetic groups
inorganic ions
coenzymes

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22
Q

prosthetic groups

A

bind tightly to become a permanent part

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23
Q

coenzyme

A

bind loosely

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24
Q

enzyme activity definition

A

indicates the rate of reaction catalysed by the enzyme expressed

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25
Q

factors that affect enzyme activity

A

temperature
ph
enzyme concentration
substrate concentration

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26
Q

why is rate not controlled

A

start particles move fast
collide making lots of enzyme substrate complexes
reaction slows as less available to collide
reaction stops when all are used up

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27
Q

inhibitors

A

a molecule that binds to enzymes to prevent them carrying out their catalytic functions
slow down rate of enzyme controlled reactions

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28
Q

competitive inhibitors

A

molecule with simular shape to active site binds
blocks substrate binding
less enzyme substrate complexes formed
reduced rate of reaction

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29
Q

non competitive inhibitors

A

bind to allosteric site causing change to tertiary structure
active site changes shape so substrate is no longer complementary
less ESC’s formed

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30
Q

reversible binding

A

binds temporarily
non covalent
enzyme goes back to normal

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31
Q

irreversible binding

A

permanent binding
covalent
permanently changed

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32
Q

product inhibition

A

product of reaction inhibits enzyme involved in that reaction
can be competitive or non competitive
always reversible

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33
Q

DNA

A

deoxyribonucleic acid
found in nucleus
carries code to make all proteins in body

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34
Q

RNA

A

ribonucleic acid
used to make proteins
3 forms - messenger , transfer, ribosomal

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35
Q

structures of nucleotide

A

phosphate
pentose sugar
nitrogenous base

36
Q

how are nucleotides linked together

A

condensation reaction
phosphate group at 5th carbon of pentose sugar forms covalent bond with hydroxyl group at 3rd carbon of pentose sugar of adjacent sugar
forms phosphodiester bond

37
Q

name of bond between nucleotides

A

phosphodiester

38
Q

pyrimidines

A

smaller bases which contain single carbon ring structures
Thymine and cytosine

39
Q

purines

A

larger bases which contain double carbon ring structures
adenine and guanine
pure as gold (Ag)

40
Q

ATP structure

A

3 phosphate groups
ribose sugar
adenine base

41
Q

formation of ADP

A

hydrolysis reaction of ATP where water used to split bond between 2nd and 3rd phosphate group releasing the phosphate group Pi and a small amount of energy

42
Q

reaction to convert ADP back to ATP

A

add energy from food to re join bond
ADP add Pi
phosphate group re joins releasing a water molecule
condensation reaction

43
Q

structure of dna

A

double helix
made of 2 anti-parallel DNA nucleotides held together by hydrogen bonds between complementary base pairs

44
Q

sense strand definition

A

contains genetic code for protein

45
Q

antisense strand definition

A

acts as a template strand for transcription
runs 3’ to 5’
complementary to sense strand

46
Q

complementary base pairing rules

A

adenine and thymine form 2 hydrogen bonds
cytosine and guanine form 3 hydrogen bonds

47
Q

which parts of dna are hydrophobic

A

nitrogenous base

48
Q

which parts of dna are hydrophilic

A

phosphate group

49
Q

chromosome definition

A

long strand of dna made up of many genes

50
Q

chromatin

A

chromosomes wrapped around histones

51
Q

histones

A

proteins dna’s wrapped around it

52
Q

gene

A

short section of dna that codes for a particular protein

53
Q

dna extraction practical method

A

crush strawberry using pestle and mortar with 20cm3 dna extraction buffer
strain into beaker using tea strainer and muslin
pour filtrate into boiling tube
add 5cm3 ethanol
let stand for 5 minutes
dna will form white precipitate on top layer
use inoculating loop to scoop out

54
Q

why is strawberry crushed

A

to break up cells

55
Q

function of adding detergent to strawberry

A

break up cell wall and phospholipid bilayer

56
Q

function of adding protease enzyme during dna extraction

A

break down histones to separate from dna

57
Q

function of adding salt during dna extraction

A

helps make it less soluble

58
Q

function of adding ethanol during dna extraction

A

to make dna become visible

59
Q

what is DNA replication and when and where does it take place

A

copying of dna
happens in the nucleus immediately before mitosis in late interphase

60
Q

semi conservative replication definition

A

each daughter DNA molecule has one new and one old strand

61
Q

DNA replication steps

A

dna helicase unwinds dna molecule and travels along it breaking the hydrogen bonds between complementary base pairs
makes 2 single strands
each strand acts as template for assemble of new complementary strand
free dna nucleotides attract to exposed bases on template strand and hydrogen bonds form between them
DNA polymerase travels along new strand catalysing the joining of nucleotides by phosphodiester bonds
each new dna molecule has one new and one old strand

62
Q

where do the free dna nucleotides come from in dna replication

A

cytoplasm

63
Q

conservative dna

A

dna copied and get one new strand

64
Q

dispersive replication

A

dna is cut into several parts and each section is copied and reattached to produce 2 molecules

65
Q

Experiment on bacteria for DNA replication

A

1- heavy nitrogen growth medium . bacteria uses heavy nitrogen to synthesis new dna
2- moved into light nitrogen medium. Bacteria uses light nitrogen to synthesis nitrogenous bases in dna. Band moves slightly up tube
3- still in light nitrogen. 2 molecules are now made of light nitrogen
if carried on more pure light nitrogen will be forms but 2 molecules will still always have only 1 strand of light

66
Q

what is the genetic code

A

code that determines the order of amino acids in each and every protein in all living things

67
Q

where is the genetic code found

A

our DNA in the nucleus
mRNA that goes to ribosome for protein synthesis

68
Q

why is there 2 versions of the genetic code

A

1st version allows you to translate dna
2nd version allows you to translate rna

69
Q

triplet

A

3 bases codes for one amino acid

70
Q

what is the genetic code described as

A

triplet
non-overlapping
degenerate
universal

71
Q

Non-overlapping for genetic code

A

each base is read in only one triplet /codon

72
Q

degenerate in terms of the genetic code

A

each amino acid has more than one triplet code that codes for it

73
Q

what does it mean by the genetic cod is universal

A

same code used for all living things

74
Q

gene

A

short section of DNA that codes for a specific protein

75
Q

why don’t ribosomes go straight into the nucleus to make the protein

A

dna might get damaged
ribosomes needs single strand whereas dna is double stranded

76
Q

overview of transcription

A

genes copied from dna to mrna
happens in nucleus

77
Q

overview of translation

A

happens in ribosomes
code on rna is used to assemble the amino acid in the correct order to make protein

78
Q

steps for protein synthesis

A

transcription and translation

79
Q

messenger RNA

A

carries code from gene to ribosome

80
Q

ribosomal RNA

A

joined with protein to form ribosome
small subunit binds to mRNA

81
Q

transfer RNA

A

amino acid on it is specific to each tRNA anticodon
brings amino acid to mRNA in translation

82
Q

steps in transcription

A

dna is unwound by dna helicase
dna helicase travels up centre of dna breaking the hydrogen bonds to form 2 separate strands
antisense strand is used as template (3’ to 5’)
free RNA nucleotides base pair with complementary bases on template strand Uracil replaces thymine
RNA polymerase catalyses formation of phosphodiester bonds
continues util end of gene
mrna leaves nucleus via nuclear pore and goes to ribosome

83
Q

where does translation occur

A

ribosome

84
Q

translation steps

A

end of mRNA binds between small and large subunits of ribosome
ribosome moves along mRNA until finds start codon
tRNA with complementary anticodon to start codon binds to mrna
another trna with complementary anticodon to nxt codon binds
the 2 amino acids then form a peptide bond
this releases the 1st amino acid
this repeats until stop codon is reached and then the ribosome becomes detached from polypeptide chain

85
Q
A