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Biology > topic 1 > Flashcards

topic 1 Flashcards

1
Q

monosaccharide

A

single sugar monomer

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2
Q

disaccharide

A

sugar made from 2 monosaccharides joined by a glycosidic bond in a condensation reaction

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3
Q

polysaccharide

A

polymer made up of long chains of monosaccharides joined by glycosidic bonds

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4
Q

what is the difference between alpha and beta glucose?

A

on alpha glucose the OH group on carbon-1 is below the plain of the ring

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5
Q

what bond/reaction joins monosaccharides?

A

condensation/glycosidic

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6
Q

what reaction splits a glycosidic bond between monomers?

A

hydrolysis reaction

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7
Q

glucose structure

A

contains 6 carbon atoms
major energy source for most cells
very soluble
main form carbs are transported around the body

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8
Q

starch structure

A

stored in plastids (leaves and potatoes)
produced from glucose in photosynthesis
broken down during respiration for energy
made of many alpha glucose molecules
amylose has a helical structure, 1-4 bonds
amylopectin is branched so more compact, 1-6
multiple chains ends - rapid hydrolysis as more attachment points for amylase enzyme

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9
Q

glycogen structure

A

insoluble
main carb storage molecule in animals and fungi
1-6 glycosidic bonds
compact so large amount of glucose is stored
stored in liver and muscle cells in animals - power respiration

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10
Q

cellulose

A

beta glucose
main component of plant cells
very high tensile strength
h-bonds form between adjacent hydrogen molecules
h-bonds between cellulose molecules form microfibrils which then form thicker fibre
fibres cross link - forms cell wall
stops cell wall bursting under pressure
allows turgidity
cannot be digested by most animals

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11
Q

triglyceride

A

one glycerol and 3 fatty acids joined by a condensation reaction where 3 water molecules are removed and an ester bond forms

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12
Q

ester bond

A

formed between the carboxyl group of a fatty acid and the hydroxyl group of glycerol in a condensation reaction

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13
Q

saturated fats

A

NO double bonds between carbon atoms
linear, lie parallel close to each other
more dense than unsaturated
solid at room temp

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14
Q

unsaturated fats

A

double covalent bonds between at least 2 carbons
cannot lie parallel
less dense than saturated
liquid at room temp

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15
Q

use of lipids

A

energy store
respiratory substrate
thermal insulation
buoyancy
electrical insulator
insoluble in water - don’t interfere with chemical reactions in cells
protect organs from mechanical shock

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16
Q

phospholipids

A

glycerol molecules with 2 hydrocarbon tails and a phosphate
phosphate is polar/hydrophilic
fatty acids are not polar/hydrophobic
form phospholipid bilayer in water

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17
Q

amino acid structure

A

r-groups control bonding between amino acids
control protein structure
polar or non-polar

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18
Q

forming proteins

A

hydrogen from amino group reacts with the hydroxyl group of the carboxyl group (of another amino acid) to form a peptide bond
water is produced in the condensation reaction

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19
Q

peptide bond

A

strong covalent bond

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20
Q

polypeptides

A

formed when many amino acids are bound togehter via a series of condensation reactions
can be several thousand amino acids
when folded its called a protein

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21
Q

protein bonding

A

ionic
disulphide
hydrogen

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22
Q

hydrogen bonding (proteins)

A

partially positive r-group and a partially negative r-group
weak bond which can be broken by increase temps or pH

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23
Q

ionic bonding (proteins)

A

r-group with a full negative charge and one with a full positive charge
stronger than hydrogen
broken by changes in pH

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24
Q

disulphide bonding (proteins)

A

R-group of 2 cysteine amino acids
very strong covalent bonds
holds together different polypeptide chains in proteins with quaternary structure

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25
Q

protein structure

A

primary
secondary
tertiary
quaternary

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26
Q

primary structure

A

linear sequence
number and order of amino acids determined by DNA sequence
only involves peptide bonding
determines 3D shape + properties of protein
varies:
number of amino acids
order of amino acids
type of amino acids used

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27
Q

secondary structure

A

hydrogen bonds between amine and carboxyl group of adjacent amino acids
most fibrous proteins have this structure
2 different types: alpha helix and b pleated sheet
- both hydrogen bonds occur between the oxygen of carboxyl group and hydrogen of amino group
- (alpha helix) 1 amino acid forms a hydrogen bond 4 places ahead of it in the chain
- (B pleated sheet) polypeptide is folded into regular pleats

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28
Q

tertiary structure

A

protein becomes folded and takes on a 3D shape
occurs in the ER
5 types of bonds holding the structure together
(ionic, hydrogen, disulphide, hydrophobic/hydrophilic interactions)
globular shape

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29
Q

quaternary structure

A

3D shape arrangment of more than one polypeptide chain
assosiation of 2 or more polypeptide chains with each other

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30
Q

fibrous proteins

A

polypeptide form long chains running next to each other
linked by disulphide cross bridges - stable + strong
structural functions a) keratin b)collagen

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31
Q

collagen

A

found in: tendons, cartilage, bone, sea anemones, egg cases of dogfish
strong
inelastic
flexible
(primary structure) repeat sequence of 3 amino acids, every 3rd amino acid is glycine
(quaternary) 3 helical polypeptides are wound very closely around each other, held by h-bonds
forms a tight coil
triple helix - tropocollagen
staggered ends so no line of weakness

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32
Q

globular proteins

A

most tertiary structure some quaternary
roughly globular
shape determines its function

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33
Q

haemoglobin

A

large globular protein
4 polypeptide chains linked by disulphide bonds
polypeptide chains arranged around an iron containing haem group

34
Q

glycoproteins

A

water reduces their viscosity
lubricants found in mucus and synovial fluids

35
Q

lipoproteins

A

important in the transport of cholesterol in the blood

36
Q

DNA

A

deoxyribonucleic acid
double helix made of 2 polynucleotides joined together by h-bonds

37
Q

RNA

A

ribonucleic acid
single stranded
mRNA, tRNA, rRNA

38
Q

purines

A

adenine and guanine
2 nitrogen containing rings

39
Q

pyrimidines

A

thymine, cytosine, uracil
single ring structure
1 nitrogen containing ring

40
Q

nucleotides

A

join together via phosphodiester bonds formed in condensation reactions

41
Q

DNA replication

A

semi conservative - uses strand from original DNA molecule as template, new DNA contains 1 old and 1 new strand
helicase
polymerase
ligase

42
Q

helicase in DNA replication

A

breaks h-bonds between base pairs
forms 2 separate strands

43
Q

DNA polymerase (replication)

A

joins adjacent nucleotides on new strand in 5’ to 3’ direction
via condensation reactions
form phosphodiester bonds

44
Q

ligase (replication)

A

leading strand replicated continuously in direction of replication fork
lagging strang is replicated in Okazaki fragments in opposite direction

45
Q

gene

A

a sequence of bases on a DNA molecule that codes for a specific sequence of amino acids to make a polypeptide

46
Q

structure of mRNA

A

long ribose polynucleotide
single stranded + linear
codon sequence is complementary to exons of 1 gene from 1 DNA strand

47
Q

structure of tRNA

A

single stranded
clover shape
anticodon at one end - binds to complementary mRNA codon
amino acid binding site at the other - amino acid corresponds to anticodon

48
Q

transcription

A

molecule of mRNA is made in the nucleus
h-bonds between complimentary bases uncoil (DNA helicase)
antisense strand is used as a template to make mRNA
sense strand
free nucleotides line up on template strand, join with adjacent nucleotides by phosphodiester bonds (DNA polymerase)
mRNA goes out of the nucleus through nuclear pore and attaches to ribosome in cytoplasm

49
Q

translation

A

amino acids join together to form a polypeptide chain
mRNA attaches to ribosome on RER
tRNA molecules binds to mRNA codon
h-bonds form between the anitcodon of tRNA and codon of mRNA
2nd tRNA molecules binds to the next mRNA codon
2 amino acids form a peptide bond
3rd tRNA molecules joins and the 1st leaves the ribosome
ATP is used to form peptide bonds
polypeptide chain is made
stops when a stop codon is reached on the mRNA

50
Q

genetic code

A

triplets of bases - codons
non overlapping - each triplet is only read once
degenerate - more than one codes for an amino acid
universal - same bases and sequencing used by all species

51
Q

effect of degenerate

A

reduces effect of mutations (deletions/insertions/substitutions)

52
Q

mutations of DNA

A

a change in base sequence may still code for the same amino acid
sickle cell anaemia - harmful base sequence change
deletions or insertions is more likely to be harmful as they create a frame shift

53
Q

start codon

A

nucleotides triplet AUG on mRNA codes for amino acid met

54
Q

stop codon

A

nucleotide triplets UAA UAG UGA which dont code for an amino acid

55
Q

introns

A

majority of DNA
consists of non-coding regions within and between genes

56
Q

extrons

A

regions of DNA that code for amino acid sequences
separated by 1 or 2 introns

57
Q

non-disjunction

A

can cause down’s syndrome and turner’s syndrome
spindle fibre snaps and 2 copes of chromosome 21 enter the egg
if egg is fertilised the zygote has 3 copies of chromosome 21

58
Q

enzymes

A

large globular proteins
tertiary structure
metabolic rate
catalyse anabolic and catabolic reactions
biological catalyst

59
Q

induced fit

A

shape of an active site changes shape in response to a substrate entering and forming an enzyme substrate complex
active site becomes even more complimentary to shape of substrate
a reaction is more likely

60
Q

what affects enzymes rate of activity

A

temperature
pH
enzyme concentration
substrate concentration

61
Q

temperature effect on enzymes

A

increases up to optimum temperature and after decreases as enzymes have denatured

62
Q

pH effect on enzymes

A

works best at optimum pH otherwise decrease until it stops

63
Q

enzyme concentration effect on enzymes

A

increase rate up to a point and then it doesn’t have an effect

64
Q

substrate concentration affect on enzymes

A

increases up to a point until all active sites are used up

65
Q

inhibitors

A

can affect enzymes when they are present
competitive or non-competitive
reversible or non-reversible

66
Q

competitive inhibitors

A

similar structure to common substrate
competition depends on concentration
can be:
reversible - increase substrate concentration reduces inhibition
irreversible - binds permanently to the active site

67
Q

non competitive

A

when inhibitor binds to the inhibitor site the shape of the active site changes and the substrate can no longer bind to it
cannot be reversed

68
Q

inorganic ions

A

required for growth and development
nitrate
phosphate
magnesium
calcium

69
Q

nitrate ions

A

make DNA and amino acids
protein for growth and repair

70
Q

phosphate ions

A

make ATP, ADP and nucleic acid

71
Q

magnesium ions

A

produce chlorrophile
photosynthesis pigment - glucose - respire

72
Q

calcium ions

A

form calcium pectate
middle lamella in plant

73
Q

water

A

partially negative - oxygen
partially positive - hydrogen
dipolar
hydrogen bonding
weak electrostatic forces

74
Q

cohesion

A

water molecules are attracted to each other
allows water to move as a continuous column of water
hydrogen bonding causes more cohesion between molecules
leads to high specific heat capacity and high latent heat of evaporation

75
Q

universal solvent

A

ionic solutions are dissolved in water
good transport medium because so many substances dissolve in it

76
Q

maximum density of 4

A

lower temps it becomes more dense
hydrogen bonds stabilise

77
Q

less dense than water

A

insulates water below + prevents freezing
provides a habitat for many animas

78
Q

cannot be compressed

A

some organisms rely on hydraulic mechanisms

79
Q

adhesion

A

water molecules are attracted to other molecules

80
Q

high surface tension

A

water molecules below the surface are more attracted to each other than the air molecules above
essential for metabolic reactions

81
Q

benefit of adhesion and cohestion

A

allows capillary action to take place

Biology (7 decks)

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