Biological Molecules Flashcards

(33 cards)

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
primary structure vs secondary protein structure
primary = a.a in polypeptide chain, secondary = H bonds between a.a in chain, this makes it a alpha helix/beta pleated sheet
26
tertiary vs quaternary structure
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
test for proteins
biurets test, add sodium hydroxide for alkalinity, copper (ll) sulfate. blue =no purple =yes
28
what are enzymes used for
proteins. biological catalysts for metabolic reactions. their active site has a specific corresponding substrate molecule
29
what is activation energy
energy for reaction to start, given off by heat, enzymes lower this thus increasing the rate of reaction
30
name the 2 models of enzyme action
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
how can you measure enzyme activity
how fast the product is made and how fast the substrate is being broken down
32
factors affecting enzyme activity - increasing
temperature, pH, (until it denatures), substrate concentration, enzymes concentration (until there is surplus of both)
33
difference between non and competitive inhibitors
``` non = bind to enzyme away from active site, changing its shape, substrate no longer fits competitive = bind to active site which stops reaction ```