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biological molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

whats a monomer and give 3 examples

A

the smaller repeated units which larger molecules are made
examples are monosaccharides amino acids and nucleotides

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2
Q

whats a ploymer and give 3 examples

A

are molecules made from a large number of monomers joined together
examples are starch protein and dna

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3
Q

whats a condensation reaction

A

it joins two molecules together with the formation of a chemical bond and involves the elimination of a molecule of water.

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4
Q

what a hydrolysis reaction

A

breaks a chemical bond between two molecules and involves the use of a water molecule

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5
Q

what the difference between a chemical bond and an intermolecular force

A

a chemical bond is a strong,lasting attraction between atoms within a molecule, whereas an intermolecular force is a weaker attraction between molecules.

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6
Q

whats a monosaccharide and give expamples

A

its the monomers from with larger carbohydrates are made.
examples are glucose, fructose and galactose

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7
Q

how to form a disaccharide

A

by a condensation reaction of two monosaccharides. this forms a glycosidic bond.

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8
Q

examples of disaccharide and how they are formed

A

glucose + glucose = maltose + water
glucose + fructose = sucrose + water
glucose + galactose = lactose + water

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9
Q

whats an isomer

A

when two molecules have the same chemical formula but a different arrangement of atoms.

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10
Q

glucoses two isomers

A

a-glucose which has oh at the bottom
b-glucose which has oh at the top

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11
Q

how are polysaccharides formed and examples

A

polysaccharides are formed by the condensation of many glucose units.

glycogen and starch are formed by condensation of a-glucose

cellulose are formed by the condensation of b-glucose

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12
Q

formula for monosaccharides and examples

A

(CH2O)n
n is number of carbons

glucose fructose and galactose are hexose sugar
ribose and deoxyribose are pentose.

they have different structures ( ring, ring simplified, straight chain)

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13
Q

test for starch

A

add iodine if it goes blue black then. its present

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14
Q

test for reducing sugar

A

heat with bendict solution
if it goes brick red then its present but it can be semi-quantitative. so can be yellow or orange

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15
Q

test for non reducing sugar

A

heat with Benedict solution and there will be no colour change. boil with hydrochloric acid then add sodium hydrogen carbonate then heat with Benedict solution and it goes brick red then its present. the only non reducing sugar is sucrose

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16
Q

starch

A

is a polysaccharide made from a-glucose
There are both unbranched and branched chains.
the unbranched has coils so is compact and stores a lot. they have 1-4 glycosidic bond and hydrogen bonds within the coil.
the branched chains have both 1-4 and 1-6 glycosidic bonds between the monomers. it has a large surface area (branches) allowing more enzymes to act upon it. starch is insoluble so water doesn’t move into it and doesn’t affect the water potential in the cell. its also large so cannot diffuse out of the cell membrane.

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17
Q

cellulose

A

is a polysaccharide made form b-glucose.
its made of straight unbranched parallel chains.
it has 1-4 glycosidic bonds. it has hydrogen bonds form between monomers. many hydrogen bonds make it rigid and have strength.
it forms microfibrils and fibrils so has additional strength.

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18
Q

glycogen

A

its a polysaccharide made form a- glucose. its branched and has both 1-4 and 1-6 glycosidic bonds.
large so doesn’t diffuse into cell membrane. insoluble so doesn’t affect water potential. coiled so is compact

19
Q

lipids

A

its not a polymer because it doesn’t have repeated monomer.
lipid has a higher H-O ratio than carbohydrates.
there is two lipids: triglycerides and phospholipids.

20
Q

triglycerides

A

it has 3 fatty acids and one glycerol. they are joined together by condensation reaction forming ester bonds and 3 water molecules. The R group for fatty acids can be saturated fatty acids, monounsaturated fatty acids or polyunsaturated fatty acids.

they have high energy because they have many c-h bonds and a low mass to energy ratio. they have high water production as it has high ratio of h-o. its waterproofing, insulation and protection over organs because its non polar as it has an even distribution of charges. non polar molecules doesn’t dissolve with polar solvents like water. this makes it hydrophobic so repels water.

21
Q

phospholipids

A

they form ester bonds form condensation reaction of glycerol and fatty acids.
they form bilayers in the cell membrane.
the bilayer has a hydrophilic head that has a glycerol and phosphate ion it points outwards. it also has a hydrophobic tail that has one unsaturated fatty acid and one saturated fatty acids it points inwards. this means only non polar molecules can pass through as polar molecules are not liquid soluble.

22
Q

test for lipids

A

add ethanol shake then add water and if present there will be a white emulsion

23
Q

amino acid

A

r
/
nh2-c-cooh
/
h
they have a variable region.
many amino acids together make a polypeptide and a peptide bond (c-n) through condensation reaction.

24
Q

protein

A

in the primary stage: sequence of amino acids and peptide bonds
secondary stage: fold into b- pleated sheet or a- helix they also form hydrogen bonds ( o-h) between the amino group and carboxylic group.
tertiary stage- it folds into a 3d shape and has hydrogen ionic and disulfide bridge( only is cystine) bonds.
quaternary stage- many polypeptide chains together.

25
Q

test for protein

A

add biuret
goes lilac if present

26
Q

what are enzymes and name its types

A

its a biological catalyst. they speed up the rate of reaction. #
they are protiens. the way the amino acids fold in the tertiary structure and the binds form make the active site.
they are anabolic ( join together)
catabolic (break down)
intracellular ( within cells)
extracellular ( outside cells)

27
Q

the induced fit model

A

substrate enter active site of enzyme
enzyme change shape slightly as substrate binds
they form enzyme product complex.
product leaves active site and the active site returns back to original shape

28
Q

how to enzymes work

A

they place stress on the bonds on the substrate so lower the activation energy

29
Q

factors that affect rate of enzyme controlled reaction and how it’s determined

A

the rate of an enzyme controlled reaction is determined by the number of enzyme substrate complexes

temperature
ph
enzyme concentration
substrate concentration

30
Q

temperature on enzyme controlled reaction

A

as temp is below optimum there is less ke is so less binding so less enzyme substrate complex
as temp increases above optimum the hydrogen bonds in the tertiary structure are overcome changing the ts shape changing the as shape so denature so less e-s complexes
at optimum its the highest so more binding and more enzyme substrate complex

31
Q

ph equation

A

-log10(h+)

32
Q

ph on enzyme controlled reaction

A

below optimum ph there is high concentration of H+ ions. change in H+ in the external solution can change the charges of amino acids so particularly affects hydrogen and ionic bonds so changes tertiary structure. so changes as so less e-s complexes

above optimum ph there is low concentration of H+ ions so this changes the charges of amino acids so partially affects hydrogen and ionic bonds so changes tertiary structure. so changes as so less e-s complexes

33
Q

enzyme concentration on enzyme controlled reaction

A

initially as the enzyme concentration increases so does the rate because the is more as so more binding so more e-s complex
however the graph then plateaus because substrate is the limiting factor so the e-s complex remain the same

34
Q

substrate concentration on enzyme controlled factor

A

initially as the substrate increases there more binding so more e-s complex

however the graph plateaus so the enzyme is the limiting factor so the e-s complex remains the same

35
Q

how to find the initial rate of reaction

A

you draw a line from 0 and up the graph
the steeper the gradient the faster the rate

36
Q

inhibitor

A

it reduces the rate of reaction
competitive inhibitor does it by blocking the as
non competitive inhibitor changes the shape of the as

37
Q

competitive inhibitor

A

it has a similar shape to the substrate so binds to the as. means fewer e-s complexes as substrates can’t bind with the as.

the graph compared to the normal is that is less steep and the rate of reaction decreases because there is less e-s complexes

38
Q

non competitive inhibitor

A

they are complementary to the allosteric site of the enzyme so it binds and changes the shape of as forever so the substrate doesnt fit so no e-s complexes

the graph compared to the normal one and ci graph is less steeper and then plateaus cux there is no e-s complexes

39
Q

dna and rna

A

deoxyribonucleic acid and ribonucleic acid are important information-carrying molecules. In all living cells, DNA
holds genetic information and RNA transfers genetic information
from DNA to the ribosomes.
ribosomes are formed from rna and protiens.

40
Q

dna structure

A

its a polymer of nucleotide
its a double helix with two polynucleotide chains ( anti-parallel) held together by hydrogen bonds between specific complementary
base pairs.
The components of a DNA nucleotide are deoxyribose, a
phosphate group and one of the organic bases adenine,
cytosine, guanine or thymine.

41
Q

two nucleodies reaction

A

A condensation reaction between two nucleotides forms a phosphodiester bond.
the phosphate and deoxyribose 3-5 phosphodiester bonds.
they are strong bonds and form the backbone

42
Q

complementary bases

A

cytosine - guanine
adenine- thymine

thymine and cytosine are with the base pyrimidine
adenine and guanine are with the base purine

ribose has one extra oxygen. and it replaces thymine
the phrase cute the pyramid

43
Q

formation of dna

A

dna codes for protiens
3 nucleiodies make a amino acid
amino acids order determine dna

44
Q

rna molecule

A

its a short polynucleotide chain

biology (1 decks)

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