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IOE > Biochemistry > Flashcards

Biochemistry Flashcards

1
Q

what are the main components of a cell membrane?

A

lipids and proteins.

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2
Q

what are the components of a phospholipid?

A
  • alcohol
  • phosphate
  • glycerol
  • 2x fatty acids.
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3
Q

for a D-glucose where would you expect to find the OH?

A

on the right

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4
Q

for a L-glucose where would you expect to find the OH?

A

on the left.

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5
Q

on a carbohydrate - you number the carbon atoms, how can you tell which carbon in number 1?

A

it is the one that is a carbonyl group. so is connected by a double bond with O and also bonded to a hydrogen.

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6
Q

if a carbohydrate has a carbon atom with a double bond to an oxygen and a single bond to a hydrogen what are they classed as?

A

aldose.

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7
Q

if a carbohydrate has a carbon atom with a double bond to an oxygen and no bond to a single hydrogen what are they classed as?

A

ketose.

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8
Q

in a haworth projection of glucose if the OH is at the bottom on the right hand side what time of sugar are they?

A

alpha glucose.

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9
Q

in a haworth projection of glucose if the OH is at the top on the right hand side what time of sugar are they?

A

beta glucose.

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10
Q

what is meant by the term mutariotation carbohydrate?

A

that is can spontaneously change between alpha and beta.

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11
Q

what is a 5 membered ring monosaccharide called?

A

furanose.

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12
Q

what is a 6 membered ring monosaccharide called?

A

pyranose.

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13
Q

what is the bond between 2 monosaccharides called?

A

glycosidic bond.

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14
Q

what 2 monosaccharides makes up sucrose?

A

glucose + fructose.

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15
Q

what 2 monosaccharides makes up lactose?

A

glucose + galactose.

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16
Q

what 2 monosaccharides makes up maltose?

A

glucose and glucose.

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17
Q

where is lactose found?

A

milk of mammals.

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18
Q

where is sucrose found?

A

in sugar cane and sugar beets.

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19
Q

what is meant by the term homopolysaccharide?

A

polysaccharide make up from the same monosaccharide.

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20
Q

what are 2 examples of homopolysaccharide?

A
  • glycogen.

- starch.

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21
Q

what is the purpose of glycogen in humans?

A

stored carbs.

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22
Q

what is glycogen made up from?

A

many glucose.

a-(1,4) linkages with a a(1,6)branched linkage every 8-10.

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23
Q

what is the main difference it the structure between glycogen and starch?

A

glycogen is very compact - large amount of carbon energy in small volume.

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24
Q

what is the purpose of starch in plants?

A

stored carbs.

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25
Q

what is unbranched starch called?

A

amylose.

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26
Q

what is branched starch called?

A

amylopectin.

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27
Q

how is cellulose different from amylose?

A

humans don’t contain enzymes to break down cellulose - so we are unable to digest it.

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28
Q

what is a carb joined with a lipid called?

A

glycolipid.

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29
Q

what is a carb joined with a protein called?

A

glycoprotein.

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30
Q

what are Glycosaminoglycans (GAGs)?

A

long unbranched polysaccharide containing a repeating disaccharide unit.

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31
Q

what are 3 examples of Glycosaminoglycans in the human body?

A
  • Dermatan sulphates (in skin/blood vessels/ heart valves)
  • Chonaritin 4 + 6 sulphates (in cartilage, bone, and heart valves)
  • Heparan sulphates (in basement membranes and components of cell structure.
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32
Q

what are the majority of GAGs in the body linked to?

A

proteins creating proteoglycans.

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33
Q

what are glycoproteins?

A

GAGS links to core proteins that are then cell-surface antigens, virus coat proteins and cell receptors.

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34
Q

what are the components of DNA?

A
  • phosphate group
  • pentose sugar (either ribose or deoxyribose)
  • nitrogenous base
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35
Q

what are the 5 bases found in cells?

A
  • adenine
  • guanine
  • thymine
  • cytosine
  • uracil.
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36
Q

what 2 bases are the derivatives of purine?

A
  • adenine

- guanine

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37
Q

what 3 bases are the derivatives of pyrimidine?

A
  • thymine
  • cytosine
  • uracil.
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38
Q

what is the structure of an amino acid?

A

a central carbon connected to:

  • hydrogen,
  • carboxyl group
  • R-group
  • amino group.
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39
Q

what part of the amino acid base structure changes for each amino acid?

A

R-group.

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40
Q

what bond is formed between amino acids?

A

peptide bonds.

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41
Q

what are the roles of lipids within the body?

A
  • structural component of biological membrane.s
  • provide energy reserves.
  • serve as vitamins and minerals
  • lipohilic bile acids aid in lipid solubilisation.
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42
Q

what are the 3 groups lipids are classified into?

A
  • fatty acids
  • cholesterol
  • lipoproteins.
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43
Q

what is the structure of a fatty acid?

A

carboxylic aid end with a long-chain hydrocarbon tail.

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44
Q

what is understood by the term saturated?

A

most hydrogens possible

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45
Q

what is understood by the term unsaturated?

A

at least one double bond between 2 carbon molecules.

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46
Q

what is the basic structure of a triacylglyceride?

A

glycerol with 3 fatty acids chains of it.

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47
Q

what is the structure of cholesterol?

A

4 rigidly fused carbon ring forming the steroid nucleus with a hydroxyl (OH) group attaching to one end and a steroid to the other.

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48
Q

what is the importance of cholesterol to a cell membrane?

A

it adds rigidity and strength against mechanical rupture.

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49
Q

what are 2 vitamins derived from steroids?

A
  • ergosterol

- vitamin D

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50
Q

what is the phospholipid found in membranes that doesn’t include glycerol?

A

-sphingomyelin.

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51
Q

is cholesterol found in prokaryotes?

A

no- it is absent.

52
Q

what is meant by the term amphipathic?

A

contains hydrophilic and hydrophobic properties.

53
Q

what is meant by the term integral membrane protein?

A

protein that is interact extensively with the bilayer.

54
Q

what is meant by the term peripheral proteins?

A

bind to surface of integral proteins - they can span the membrane with alpha helices.

55
Q

what is meant by the term bacteriorhodopsin?

A

alpha spanning helices in contact with hydrocarbon core (aka the tails) or with other alpha spanning helices.

56
Q

what type of he helices fold in such a way to form a hollow cylinders through the phospholipid bilayer of cell membranes?

A

beta helices that found bacterial porin.

57
Q

what type of environment are amino acids showing a more negative value most likely to be found?

A
  • aqueous environments.
58
Q

what is membrane movement/fluidity controlled by in the phospholipid bilayer?

A

fatty acid composition (more unsaturated- not as tightly packed)and cholesterol content (.

59
Q

how can the differences between cell membranes in prokaryotes be identified?

A

using gram stain.

60
Q

how can molecules transport across the plasma membrane?

A
  • diffusion
  • transporter proteins
  • channel proteins.
61
Q

what are prokaryote?

A

bacterial small single-cell organisms.

62
Q

what is the difference between prokaryotes and eukaryotes?

A

prokaryotes don’t contain organised membranous internal structures and transcription and translation can occur simultaneously.

63
Q

what are Eukaryotes?

A

all plant and animal cells

swell as algae, fungi and protozoa.

64
Q

what is the endosymbiosis theory?

A

how different organelles came into the cell - evolution.

65
Q

what is the purpose of the cytoskeleton in eukaryotes?

A

gives the cell structural integrity and allows for locomotion, transport and cell division.

66
Q

what does the cytoskeleton in eukaryotes consist of?

A
  • actin filaments
  • intermediale filaments
  • tubules filaments.
67
Q

what are the stages of mitosis?

A

1) prophase (present)
2) metaphase (middle)
3) anaphase (appart)
4) telophase (two)

68
Q

what is meiosis?

A

making of a daughter cells with half the number of chromosomes. (making a haploid daughter cell)

69
Q

how do viruses multiply?

A

hijack other cells ‘machinery’ and get them to replicate. /

70
Q

what is an example of a DNA virus?

A

poxvirus

71
Q

what are examples of a RNA virus?

A
  • HIv
  • mumps
  • influenza
  • common cold.
72
Q

how is Lysogeny (budding) carried out by viruses?

A
  • viruses injects DNA into host cell
  • virus DNA integrates with host cell DNA
  • cell goes through mitosis replicating infected DNA
  • phase induction happens with host immune system is down.
  • viral DNA comes away from host DNA, destroys the host DNA, hijacks the cells functions replicating itself until the cell explodes with many viruses.
73
Q

what are prions?

A

proteins in the brain converted leading to brain lesions.

74
Q

what kind of disease can prions cause?

A
  • BSE (mad cow disease)

- New variant CJD (human form of BSE)

75
Q

what is different about prions when compared to other cells?

A
  • very heart and UV-irradiation resistant.

- cannot be autoclaved.

76
Q

how many different types of amino acid are there?

A

20

77
Q

what is an example of a polar molecule? and what type of molecule do they tend to bond with?

A

Water is a polar molecule.

- tends to form hydrogen bonds with other water molecules or other polar molecules.

78
Q

what is mean by the term polar molecule?

A

more electro charged at the top.

79
Q

what is meant by theorem apolar molecule?

A

electo distribution is equal.

80
Q

what is an example of an apolar molecule?

A

methane.

81
Q

where are many essential amino acids humans need found?

A

in meat.

82
Q

why is diet so important regarding amino acids?

A

as humans cannot synthesis 9 essential amino acids so they need to be provided by diet.

83
Q

how are proteins primarily folded?

A

nonpolar sidedchains in the centre as they are hydrophobic.

polar side chains o the outside as they can form hydrogen bonds to water.

84
Q

what do most polypeptide chains start with?

A

methionine (AUG)

85
Q

what are the 4 folded polypeptide chain structures?

A
  • alpha helices
  • beta sheets
  • turns
  • loops.
86
Q

what causes the alpha helices folding in polypeptide chain structures?

A

hydrogen bonds to ensure that the hydrophobic non polar side chains are the the centre.

87
Q

are beta sheet arranged parallel, antiparallel or both in folded polypeptide chains?

A

both.

88
Q

is there any order to a proteins tertiary structure?

A

not at first but then tried to reduce energy when folding.

89
Q

what is most often on the surface of proteins tertiary structures?

A

charged amino acid residues.

90
Q

what is a proteins quaternary structure?

A

more than 1 polypeptide chain.

91
Q

what is an example of a protein with more than 1 polypeptide chain?

A

Insulin.

92
Q

what is meant by the term transcription in gene expression?

A

the synthesis of RNA from a DNA template.

93
Q

what is meant by the term translation in gene expression?

A

the synthesis of proteins using RNA

94
Q

what is tRNA?

A

transfer RNA.

95
Q

what is the structure of tRNA?

A

amino acids attached to 3’ end.

anticodon is the template recognition site.

96
Q

what are the 3 main things genetic code has to be?

A
  • redundant
  • unambiguous
  • universal.
97
Q

how is genetic code reductant?

A

several different triple codons sequence can encode for the same amino acid.

98
Q

how is genetic code unambiguous?

A

each codon can only encode 1 specific amino acid (ora START/ STOP)

99
Q

how is genetic code universal?

A

all living organisms use the same genetic code.

100
Q

how are proteins synthesised?

A

by the successive addition of amino acids to the carboxyl terminal.

101
Q

what are ribosomes?

A

RNA/protein hybrid structures.

102
Q

how many tRNA binding sites do ribosomes have?

A

3.

103
Q

why do ribosomes have 3 binding sites?

A

to bridge the 30s and 50s subunits.

104
Q

in what part of the ribosome has a tunnel allowing the growing polypeptide chain to extrude though?

A

50s subunits.

105
Q

what is the wobble hypothesis?

A

allows tRNA molecules to recognise more than one codon.

106
Q

what do many antibiotics do the protein synthesis?

A

inhibit it.

107
Q

what is the difference between prokaryotic mRNA and eukaryotic mRNA?

A

prokaryotic mRNA code for multiple proteins. where are eukaryotic mRNA only codes for one gene

108
Q

how is translation very accurate?

A

have a proof-reading mechanism.

109
Q

what makes the backbone of DNA?

A

sugar and phosphate.

110
Q

what is DNA replication classed as semi-conservative?

A

new stand of DNA is made up go one new and one old (original) stand of DNA.

111
Q

what does the enzyme Helices do in DNA replication?

A

‘unzipping’ - separates the 2 DNA strands.

112
Q

what does the enzyme DNA polyerase do in DNA replication?

A

builds the new stand of DNA - binds to the primer to know where to start and adds bases from 5’-3’

113
Q

what does the enzyme Primase do in DNA replication?

A

makes the primes - starts of the replication with some RNA fragments.

114
Q

what does the enzyme DNA ligase do in DNA replication?

A

seals up the fragments creating a continuous stand.

115
Q

how is the leading stand in DNA replicated?

A
  • after helicase has creating a replication form
  • primase makes the primer
  • DNA polymerase builds the rest of the strand in the 5’-3 direction.
116
Q

how is the lagging stand in DNA replicated?

A
  • after helicase has creating a replication form
  • primase makes the primer
  • DNA polymerase builds a small strand in the 5’-3 direction. (this small stand = okazaki fragment)
  • primase makes another primer further down the stand.
  • DNA polymerase creates another okazaki fragment.
  • this continues until the stand is complete.
  • exonuclease then removes the RNA primers
  • DNA polymerase then fills in the gaps left behind with DNA bases.
  • finally DNA ligase seals up the fragments in both stands - creating a continuous strand.
117
Q

what is the difference between RNA synthesis and DNA synthesis?

A

RNA synthesis is carried out by RNA polymerase, and it only requires a template not a primer.

118
Q

is DNA negatively or positively charged?

A

negatively.

119
Q

why do histone proteins bind to DNA?

A

because they are positively charged.

120
Q

how many times can a cell divide before it dies? and what is the only exception?

A

50-70 times.

but sperm cells can divide unlimited amounts.

121
Q

why many the telomerase enzyme be needed during DNA replication of the lagging strand?

A

as there may not be enough primer for all amino acids so the telomerase enzyme will extend 3’ end to allow extension of the 5’ end.

122
Q

when are the only times that the telomerase enzyme is used?

A
  • foetal development - due to rapid cell division

- cancer cells - ‘immortal’ cells

123
Q

what are 3 examples of a promoter in DNA replication and what is its purpose?

A

examples = TATA box / CAAT box / GC box.

recognition sequence immediately upstream of the transcription start site.

124
Q

what is gene splicing?

A

DNA is cut and further DNA is added - this allows organisms to produce useful products eg insulin, allowing for diversity.
but it can result in disease.

125
Q

what are the factors involved in regulation of gene expression?

A
  • chromatin remodelling (unfolding of DNA)
  • Enhancers (signalling sequence of nucleotide)
  • modification (suppress the gene)

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