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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
protein structure
primary secondary tertiary quaternary
26
primary structure
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
27
secondary structure
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
28
tertiary structure
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
29
quaternary structure
3D shape arrangment of more than one polypeptide chain assosiation of 2 or more polypeptide chains with each other
30
fibrous proteins
polypeptide form long chains running next to each other linked by disulphide cross bridges - stable + strong structural functions a) keratin b)collagen
31
collagen
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
32
globular proteins
most tertiary structure some quaternary roughly globular shape determines its function
33
haemoglobin
large globular protein 4 polypeptide chains linked by disulphide bonds polypeptide chains arranged around an iron containing haem group
34
glycoproteins
water reduces their viscosity lubricants found in mucus and synovial fluids
35
lipoproteins
important in the transport of cholesterol in the blood
36
DNA
deoxyribonucleic acid double helix made of 2 polynucleotides joined together by h-bonds
37
RNA
ribonucleic acid single stranded mRNA, tRNA, rRNA
38
purines
adenine and guanine 2 nitrogen containing rings
39
pyrimidines
thymine, cytosine, uracil single ring structure 1 nitrogen containing ring
40
nucleotides
join together via phosphodiester bonds formed in condensation reactions
41
DNA replication
semi conservative - uses strand from original DNA molecule as template, new DNA contains 1 old and 1 new strand helicase polymerase ligase
42
helicase in DNA replication
breaks h-bonds between base pairs forms 2 separate strands
43
DNA polymerase (replication)
joins adjacent nucleotides on new strand in 5' to 3' direction via condensation reactions form phosphodiester bonds
44
ligase (replication)
leading strand replicated continuously in direction of replication fork lagging strang is replicated in Okazaki fragments in opposite direction
45
gene
a sequence of bases on a DNA molecule that codes for a specific sequence of amino acids to make a polypeptide
46
structure of mRNA
long ribose polynucleotide single stranded + linear codon sequence is complementary to exons of 1 gene from 1 DNA strand
47
structure of tRNA
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
transcription
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
translation
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
genetic code
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
effect of degenerate
reduces effect of mutations (deletions/insertions/substitutions)
52
mutations of DNA
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
start codon
nucleotides triplet AUG on mRNA codes for amino acid met
54
stop codon
nucleotide triplets UAA UAG UGA which dont code for an amino acid
55
introns
majority of DNA consists of non-coding regions within and between genes
56
extrons
regions of DNA that code for amino acid sequences separated by 1 or 2 introns
57
non-disjunction
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
enzymes
large globular proteins tertiary structure metabolic rate catalyse anabolic and catabolic reactions biological catalyst
59
induced fit
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
what affects enzymes rate of activity
temperature pH enzyme concentration substrate concentration
61
temperature effect on enzymes
increases up to optimum temperature and after decreases as enzymes have denatured
62
pH effect on enzymes
works best at optimum pH otherwise decrease until it stops
63
enzyme concentration effect on enzymes
increase rate up to a point and then it doesn't have an effect
64
substrate concentration affect on enzymes
increases up to a point until all active sites are used up
65
inhibitors
can affect enzymes when they are present competitive or non-competitive reversible or non-reversible
66
competitive inhibitors
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
non competitive
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
inorganic ions
required for growth and development nitrate phosphate magnesium calcium
69
nitrate ions
make DNA and amino acids protein for growth and repair
70
phosphate ions
make ATP, ADP and nucleic acid
71
magnesium ions
produce chlorrophile photosynthesis pigment - glucose - respire
72
calcium ions
form calcium pectate middle lamella in plant
73
water
partially negative - oxygen partially positive - hydrogen dipolar hydrogen bonding weak electrostatic forces
74
cohesion
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
universal solvent
ionic solutions are dissolved in water good transport medium because so many substances dissolve in it
76
maximum density of 4
lower temps it becomes more dense hydrogen bonds stabilise
77
less dense than water
insulates water below + prevents freezing provides a habitat for many animas
78
cannot be compressed
some organisms rely on hydraulic mechanisms
79
adhesion
water molecules are attracted to other molecules
80
high surface tension
water molecules below the surface are more attracted to each other than the air molecules above essential for metabolic reactions
81
benefit of adhesion and cohestion
allows capillary action to take place

Biology (7 decks)

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