Biological Molecules Flashcards

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1
Q

how are polymers formed

A

monomers join a chemical bond by a condensation reaction which releases a molecule of water

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2
Q

how are polymers broken down

A

hydrolysis, water is used to break down the chemical bond.

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3
Q

monosaccharides: what type of sugar is glucose and what are its isomers

A

a hexose sugar, it has 6 carbon atoms in each molecule. alpha and beta glucose. alpha has the OH at the bottom and H at the top

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4
Q

disaccharies: how are they formed and what bond is created

A

monosaccharides form a glycosidic bond by a condensation reaction and

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5
Q

what monosaccharides form sucrose, lactose and maltose

A

sucrose = glucose+fructose lactose = glucose+galactose maltose = 2x alpha glucose

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6
Q

what is the reducing sugar test

A

eg all monosaccharides + lactose, maltose. Add blue benedict’s reagent, boil in water bath, change in colour = reducing sugar. green - yellow - brick red.

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7
Q

what is the non reducing sugar test

A

eg sucrose. add benedict’s reagent, hydrochloric acid and boil in a water bath. neutralise with sodium hydrocarbonate. add benedicts reagent again. blue = non-reducing sugar. this method can be used to get a reducing sugar out of a non-reducing sugar solution.

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8
Q

why use a colorimeter when using benedict’s test

A

to test the concentration of precipitate. it does this by absorbing the remaining benedict’s reagent

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9
Q

what is starch used for in plants

A

the alpha glucose polysaccharide is broken down by hydrolysis to make amylose and amylopectin to use for energy

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10
Q

what is amylose used for

A

long, unbranched, coiled, compact, great for storage

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11
Q

what is amylopectin use for

A

long, branched so enzymes break glycosidic bonds easily = easy glucose release

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12
Q

what is good about starch

A

insoluble in water so doesn’t affect water potential which makes it good for storage

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13
Q

what is the structure and function of gylcogen

A

excess glucose turns into glycogen. many branches of alpha glucose, compact and quick release of energy for mammals

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14
Q

cellulose structure and function

A

long, unbranched, beta-glucose chains. cellulose chains joined by hydrogen bonds which form strong fibres called microfibrils = support in plant cell walls

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15
Q

iodine test for starch

A

add iodine, blue/black = starch. brown/orange = no starch

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16
Q

lipids: structure of triglycerides

A

one molecule of glycerol and 3 fatty acid molecules (a tail) called hydrocarbons. tail in hydrophobic, so insoluble in water. ester bonds formed between FA and glycerol by condensation reaction

17
Q

difference between un/saturated fatty acid

A
un = have double bonds between carbon atoms
sat = no double C bonds, is saturated with Hydrogen
18
Q

structure of a fatty acid

A

O = C - HO - R(variable hydrocarbon tail)

19
Q

structure of a phospholipid

A

found in cell membrane, 2 FA , 1 glycerol, 1 phosphate group (hydrophilic)

20
Q

properties of lipids

A
triglycerides = storage, insoluble, don't affect water potential
phospholipids = bilayer of cell membrane, not easy for water soluble molecules to pass through the hydrophobic centre layer
21
Q

emulsion test for lipids

A

shake sample with ethanol, pour into water, lipid shows as a milky emulsion above the water

22
Q

what are proteins made from

A

amino acids, 2x a.a = dipeptide 2+x a.a = polypeptide

23
Q

structure of a amino acids

A

carboxcylic acid, r group, amine group. theres only 20 amino acids, their r groups is the only difference

24
Q

how are di/polypeptides formed

A

condensation reaction forms a dipeptide bond. hydrolysis breaks this down

25
Q

primary structure vs secondary protein structure

A

primary = a.a in polypeptide chain, secondary = H bonds between a.a in chain, this makes it a alpha helix/beta pleated sheet

26
Q

tertiary vs quaternary structure

A

tertiary = coiled a.a chain, more H bonds and now ionic bonds form. Disulfide bridges form between 2 cysteine molecules quaternary = made of more than one polypeptide chain eg haemoglobin

27
Q

test for proteins

A

biurets test, add sodium hydroxide for alkalinity, copper (ll) sulfate. blue =no purple =yes

28
Q

what are enzymes used for

A

proteins. biological catalysts for metabolic reactions. their active site has a specific corresponding substrate molecule

29
Q

what is activation energy

A

energy for reaction to start, given off by heat, enzymes lower this thus increasing the rate of reaction

30
Q

name the 2 models of enzyme action

A

lock and key, induced fit is more accurate = substrate has to be specific to active site and morphs a.s into the correct shape

31
Q

how can you measure enzyme activity

A

how fast the product is made and how fast the substrate is being broken down

32
Q

factors affecting enzyme activity - increasing

A

temperature, pH, (until it denatures), substrate concentration, enzymes concentration (until there is surplus of both)

33
Q

difference between non and competitive inhibitors

A
non = bind to enzyme away from active site, changing its shape, substrate no longer fits
competitive = bind to active site which stops reaction