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what Is a monomer
small units that make larger molecules
what is a polymer
made from large number of monomers and chemically bonded
examples of monomers
monosaccharides , amino acids , nucleotides
what is condensation reaction
joins 2 monomers together with formation of covalent bond and involve elimination of water
what is hydrolysis reaction
breaks covalent bonds between 2 monomer
involve use of water molecule
describe molecules of life
all contain carbon, hydrogen, oxygen
these are organic
can be grouped into 4 types, carbohydrates, lipids , proteins , nucleic acids
which make up biochem process of life
what can the monomer of glucose make polymers of
starch, cellulose , glycogen
what can the monomer of amino acids make a polymer of
protein
what can the monomer of nucleotides make a polymer of
DNA & RNA
examples of carbohydrates
monosaccharides, disaccharides, polysaccharides
examples of monosaccharides which are monomers
glucose
fructose
galactose
examples of disaccharides (dimers)
sucrose
maltose
lactose
examples of polysaccharides (polymers)
starch
cellulose
glycogen
describe glucose
exist as 2 isomer alpha and beta
found in all 3 polysaccharides
for the drawing, the right side is swapped for beta
what do molecules of life all contain
carbon, hydrogen and oxygen
all organic
what 4 groups can carbon hydrogen and oxygen be grouped into
carbohydrates, lipids, proteins, nucleic acids
describe carbohydrates
respiratory substrate
provides energy for cells
used for structure in cell membrane and cell wall in plants
describe lipids
respiratory substrate
provide energy for cells
form a bilayer in cell membrane
make up some hormones
describe proteins
main component of many cellular structure
form enzyme & chemical messengers
describe nucleic acid
form polymers (DNA & RNA)
which makes up genetic material of organisms
codes for sequence of amino acids
which make up all proteins
what are long chains of sugar units called
saccharides
what is a single monomer , pair of monomers and many called and what bonds join them together
monosaccharide
disaccharide
polysaccharide
glycosidic bonds in condensation reaction
what bonds is formed from condensation reaction between 2 monosaccharides
glycosidic bond
how is a disaccharide formed
condensation of 2 monosaccharides
how is the disaccharide maltose formed
condensation of 2 glucose molecules
how is the disaccharide sucrose formed
condensation of glucose and fructose
how is the disaccharide lactose formed
condensation of glucose and galactose
how are polysaccharides formed
condensation of many glucose units
how is glycogen and starch formed
condensation of alpha glucose
how is cellulose formed
condensation of beta glucose
describe structure of glycogen
long branched chains w lots of side branches
glycosidic bonds = 1-6
large but compact, maximising amount of energy stored
properties of glycogen
lots of branches increases SA, so enzyme can hydrolyse glycosidic bonds
which allows glucose release quickly
insoluble , doesn’t affect water potential of cells & can’t diffuse out cells
uses of glycogen
animal store excess glucose as glycogen in muscles and liver
glycogen= energy store, can be hydrolyse to release glucose quick for respiration
describe structure of starch
mix of 2 polysaccharide , amylose & amylopectin
amylose=long & unbranched , forms coils
amyloplectin=long, branched cuz of 1-6 glycosidic bond
properties of starch
amylose=coiling so is compact & store more in a smaller place
amylopectin=branches increase SA for enzyme to hydrolyse glycosidic bonds
which allows quick release of glucose
insoluble , won’t affect cell water potential
uses of starch
plants use to store excess glucose
cuz its too big to leave cells
starch can be hydrolyse to release glucose for respiration
describe structure of cellulose
long
unbranched
straight chains
glycosidic bonds 1-4
cellulose chain link by H bonds between glucose molecules in each chain
which forms thicker fibres (microfibrils)
component of cell walls in plant
properties of cellulose
H bonds between cellulose make microfibril really strong
but its still flexible allowing to provide support
uses of cellulose
major structural component
provides support
allows cell to become turgid
which also helps maximise SA of plants for photosynthesis
formula for monomer & trisaccharide
C6H1206
C18H32016
Describe lipids
biological molecules made from carbon, hydrogen , oxygen
only soluble in organic solvents
main types = triglycerides & phospholipids
roles of lipids
energy source
waterproofing
insulation
protection
describe the role of lipid as an energy source
can be a reactant in respiration to release energy
to make ATP
describe the role of lipid for waterproofing
its insoluble
creates layer around plants & animals for water retain
describe the role of lipid as an insulator
poor conducts of heat & electricity
describe the roles of lipid for protection
protects around delicate organs
describe triglyceride structure
glycerol molecule & 3 fatty acids
ester bond formed in condensation between each 3 OH group on glycerol & OH group of each fatty acid chain
non polar
describe phospholipid structure
glycerol, phosphate group, 2 fatty acid chain
ester bond formed by condensation reaction between 2 OH group on glycerol & OH group of each fatty acid chain
describe saturated lipid
found in animal fats
no carbon carbon double bond
describe unsaturated lipid
in plants
carbon-carbon double bond
can bend- so can’t pack together tightly so liquid at room temp
describe triglycerides fatty acid chain
hydrophobic so insoluble in water
so doesn’t affect water potential
why is triglyceride good energy store
high ratio energy storing C-H bonds to C
in small space
when hydrolyse lots of energy released
good for animals carrying less mass
why does triglyceride release water when oxidised and why’s this good
high ratio of H-O atoms
source of water for organisms in dry environment
properties of phospholipid
phosphate head = hydrophilic
fatty acid = hydrophobic
so forms micelles in water contact
so they’re polar & can form bilayers making up membranes
what can phospholipids form and the importance of this
can form glycolipids w carbohydrates
which is important on cell surface membrane for cell recognition
what is liposome for
transport water soluble substances in cells
what is micelles for
transport of lipid soluble substances
describe phospholipid bilayer
head = hydrophilic but tail=hydrophobic
in water form double layer
head face towards water , tail = opposite
centre=hydrophobic ——> so water soluble substance can’t easily pass
creates barrier & solution separation
describe water
polar molecule due to uneven distribution of charge
liquid at room temp
BP = 100 degrees
Hydrogen bonds
why is water polar molecule
uneven distribution of charge
unequal sharing of electron give H2O molecule slightly negative charge near its oxygen
and slightly positive charge near H atoms
describe water being liquid at room temp
mostly small molecules like water = gas at room temp
but interactions between water molecules = stronger
describe the hydrogen bonds in water
result of polarity
individually weak
collectively strong
properties of water
its a metabolite
its a solvent
has high specific heat capacity
has high latent heat of vaporisation
H2O molecules are cohesive
describe water as a metabolite
metabolism= collective name of them reaction in organism
metabolite= chemicals involved in metabolism
its metabolite in reactions like condensation, hydrolysis —→ usednin forming & breaking bonds
describe water as a solvent
good solvent cuz its polar—→ allows ions & polar molecules to dissolve easy as they’re attracted to poopsoite charges on H2O molecules
ionic compounds & polar substance dissolve in h2o—> so them reaction can happen, substance can be transported
non polar like lipid & v large molecules aren’t soluble in water
describe water having high specific heat capacity
can absorb lots of energy without changing temperature by much
why does water have high specific heat capacity
H20 molecules stick together with H bonds
so lots energy required to break these bonds
so H20 can act as a temperature buffer
benefits of water having high specific heat capacity
can act as a temp buffer
help maintain stable aquatic system
help organism maintain consistent temp , therefore maintaining consistent activity
describe water having high latent heat or vaporisation
takes lots energy to evaporate 1kg of h20
why does water have high latent heat
lots energy required to overcome H bonding between h20 molecules
describe the effect of having high latent heat in terms of sweating
sweating is effective means of cooling
cooling effect with little water loss
describe h20 molecules being cohesive in water
H bonds make H2O MOLECULES STICK TOGETHER
benefit of h20 molecules being cohesive
chains of h2o can be pulled up xylem
causes surface tension to provide habitat to support ecosystem
describe the property of solid water being less dense than liquid
when h20 freeze, h bonds become longer
so particles more spread out
and in a crystalline structure compared to when liquid
how is solid water being less dense than liquid make it a useful property
frozen water can provide habitats to support ecosystems
what is the monomener making up proteins
amino acids
how are peptide bonds formed
condensation reaction between 2 amino acids
peptide bonds form between amine group of 1 amino acid & carboxyl group of other
h2o molecule released
how is dipeptide bond formed
2 amino acids join by condensation
carboxyl group of 1 amino acid react w amino group of another
how is polypeptide bond formed
condensation of many amino acids
describe proteins
can be globular or fibruous
catalyse reactions or movement of substance across phospholipid bilayer
enzymes made of proteins
describe globular proteins
have role in cell signalling
describe role of fibrous protein
have structural role
describe protein struc
polymers made of monomers of amino acids
20 amino acids
contain hydrogen, oxygen, also nitrogen
R group made of fdiff elements
what does the r group in proteins cause and mean
means they have diff properties & interact with other molecules diff
affects protein shape
describe primary struc of protein
the sequence of amino acids joined by peptide bonds in polypeptide chains
contain initial sequence of amino acid
so determine protein function
describe secondary struc of protein
polypeptide chain coil into alpha helix or fold into beta pleated sheets
structures held bh H bonds, forming between amino acids in chain
many H bonds make struc stable
describe tertiary struc of protein
3d shape of polypeptide chain
specific shape created cuz of sequence of amino acids
H bonds , ionic bonds , covalent form between R groups
why does change of amino acids affect secondary and tertiary structure
cuz bonds would form in diff places
changing temp/ph of solution the protein is in could also affect bonds, which affects secondary and tertiary struc so function affected
describe quaternary struc of protein
proteins made from more than 1 polypeptide chain
H bonds , ionic, covalent form between polypeptide chain
to hold quarternary struc together
enzyme function
increase rate of reaction by lowering activation energy
also catalyse specific metabolic reaction at cellular level
eg respiration, photosynthesis
structure of enzymes and how the shape is determined
3D tertiary structured globular proteins
shape determined by primary sequence of amino acids
describe active site of enzyme
has specific tertiary structure which is complimentary to substrate
only binds to certain substrate
ES complex form when enzyme bind to substrate
what happens when enzyme reaction done
product leaves active site
enzyme goes and makes more ES complex
how do enzymes speed rate of metabolic reaction
lowering activation energy
usually allow reaction to happen at lower temperature than without enzyme
how does allowing the reaction to happen at lower temp with enzyme increase rate
enzyme either hold substrate close tg
reducing repulsion & allowing them to bond easier/ put more strain on bonds of substrate
allowing them to break apart easier
describe lock and key enzyme model
shape of active site = exactly complimentary to substrate
substrate fit in exactly when they collide, forming ES complex
describe induced fit enzyme model
shape of active site=not exactly complmentary to substrate
when substrate collide w enzyme , active site can slightly change shape to fit around substrate
& form ES complex
describe how increasing enzyme conc affects rate
rate of reaction increase
cuz more active sites for substrate to bind to
increasing beyond certain point has no effect on rate
cuz there’s more active sites than substrate
substrate can become limiting factor
describe how increasing substrate conc affects rate
rate increase
cuz more substrate molecules
more collisions=more ES complex
rate slows as enzyme conc becomes limiting fac
rate follows curve cuz when lots active sites alr occupied, there’s reduced chance of successful collision of enzyme & active site
describe how increasing temp affects rate
initially rate increases
cuz molecules have more KE= move faster
increasing num of successful collisions
increasing num of ES complex
once optimum temp reach rate go down
at high temp enzyme denature→tertiary struc of AS permanently changed
heat energy broke bonds holding T struc so AS not complimentary , so no more ES complex
cuz substrate can’t fit