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ap bio > 3.2-6 macromolecules > Flashcards

3.2-6 macromolecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

monomers definition

A

small organic
used for building blocks of polymers
connects with condensation reaction (dehydration synthesis)

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2
Q

polymers definition

A

long molecules of monomers
many identical or similar blocks linked by covalent bonds

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3
Q

macromolecules

A

giant molecules
2+ polymers bonded together

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4
Q

dehydration synthesis (condensation reaction) properties

A

make polymers
monomers –> polymers
A + B –> AB
produces H2O

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5
Q

hydrolysis properties

A

breakdown polymers
polymers –> monomers
AB –> A + B
uses H2O

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6
Q

hydrolysis definition

A

breaking down a polymer

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7
Q

carbohydrates properties

A

fuel and building material
includes simple sugars (fructose) and polymers (starch)
ratio: CH2O

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8
Q

monosaccharides definition

A

monomers

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9
Q

polysaccharides purpose

A

storage (plants-starch, animals-glycogen)
structure (plant-cellulose, arthropod-chitin)

differs in position and orientation of glycosidic linkage

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10
Q

two types of glucose

A

starch: α glucose
cellulose: β glucose

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11
Q

structural polysaccharides

A

cellulose and chitin (exoskeleton)

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12
Q

fats/oils (triglyceride) purpose and properties

A

store energy
glycerol (3C alcohol) + 3 fatty acids
saturated, unsaturated, polysaturated

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13
Q

steroids structure

A

4 fused carbon rings (isoprene) + ??

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14
Q

how are different steroids created?

A

attaching different functional groups to rings

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15
Q

different structure creates

A

different function

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16
Q

phospholipid structure

A

glycerol + 2 fatty acids + PO4

hydrophobic fatty acid tails
hydrophilic PO4 head

steroid backbone

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17
Q

hydrophobic/hydrophilic interactions create

A

phospholipid bilayer

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18
Q

waxes are made up of

A

glycerol and alcohol (monomer)

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19
Q

nucleic acid function

A

store hereditary info

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20
Q

DNA properties

A

Double-stranded helix
N-bases: A, G, C, Thymine
Stores hereditary info
Longer/larger
Sugar: deoxyribose

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21
Q

RNA properties

A

Single-stranded
N-bases: A, G, C, Uracil
Carry info from DNA to ribosomes
tRNA, rRNA, mRNA, RNAi
Sugar: ribose

various functions during gene expression

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22
Q

nucleotide definition

A

monomer of DNA/RNA

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23
Q

nucleotides are made of

A

sugar + phosphate + nitrogen base

24
Q

information flow in a cell

A

DNA –> RNA –> protein

25
Q

proteios meaning

A

first or primary

26
Q

proteins contain what elements?

A

c, h, o, n, s

27
Q

proteins take up what percentage of dry weight in a cell?

A

50%

28
Q

proteins functions

A

enzymes
defense
storage
transport
hormones
receptors
movement
structure

29
Q

enzymatic protein function

A

selective acceleration of chemical reactions

30
Q

defensive proteins function

A

protection against disease

31
Q

storage proteins function

A

storage of amino acids

32
Q

transport proteins function

A

transport of substances

33
Q

hormonal proteins function

A

coordination of an organism’s acitivities

34
Q

receptor proteins function

A

response of cell to chemical stimuli

35
Q

contractile and motor protein functions

A

movement

36
Q

structural proteins function

A

support

37
Q

primarily level of protein structure

A

amino acid sequence
20 different amino acids

38
Q

what bonds link amino acids?

A

peptide bonds

39
Q

amino acid properties

A

hydrophobic non polar r-group
hydrophilic polar r-group
ionic (acids and bases)

40
Q

amino acid

A

r-group: side chains
amino: -NH2
acid: -COOH

41
Q

secondary level of protein structure

A

3d shape
hydrogen bonding between oxygen of carboxyl of one amino acid and hydrogen of another

42
Q

what shapes does the secondary level of protein structure form?

A

Alpha (α) helix, Beta (β) pleated sheet

43
Q

4 basic principles of protein folding

A

Hydrophobic/nonpolar amino acids buried in interior of protein (hydrophobic interactions)

Hydrophilic/polar amino acids exposed on surface of protein (hydrogen bonds)

Acidic and basic amino acids form salt bridges (ionic bonds)

Cysteines can form disulfide bonds

44
Q

tertiary level of protein structure

A

bonding between r-groups (side chains) of amino acids

45
Q

tertiary level of protein structure bonds

A

hydrogen
ionic
disulfide bridges
van der Waals interactions

46
Q

quaternary level of protein structure

A

2 or more polypeptides bonded together

47
Q

amino acid process

A

amino acid –> polypeptides –> protein

48
Q

chaperoning purpose

A

assist in proper protein folding

49
Q

protein _ and _ are sensitive to chemical and physical conditions

A

structure, function

50
Q

what conditions are not optimal for proteins?

A

changes in pH and temperature

51
Q

what happens if proteins are restored to original conditions after changes in temp or pH?

A

renaturation or permanent denaturing

52
Q

carbohydrates components

A

C, H, O

53
Q

carbohydrates examples

A

mono, di, polysaccharides

54
Q

carbohydrates functions

A

fuel: carbon sources that can be converted to other molecules or combined into polymers

strengthen plant cell walls

stores glucose for energy

strengthens exoskeletons and fungal cell walls

55
Q

lipid examples

A

triacylglycerols
phospholipids
steroids

56
Q

lipids functions

A

important energy source
lipid bilayer
component of all cell membrane (cholesterol)
signaling molecules that travel through the body (hormones)

57
Q

proteins components

A

amino and monomer (20 types)

ap bio (11 decks)

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