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chapter five Flashcards

structure and function of macromolecules

1
Q

polymers

A

large compounds made of many monomers

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2
Q

what are the four types of macromolecules?

A

carbs, proteins, lipids, nucleic acids

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3
Q

dehydration/condensation reaction

A

synthesizing a polymer, removes a water molecules forming a new bond

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4
Q

hydrolysis

A

breaking down a polymer, adds a water molecules breaking a bond

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5
Q

carbohydrates

A

fuel and building materials

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6
Q

what is the monomer of carbs?

A

monosaccharides

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7
Q

general formula of carbs?

A

C6H12O6

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8
Q

glucose typically forms what shape?

A

ring form with 3-7 carbons

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9
Q

disaccharide or two monosaccharides = ?

A

glycosidic linkage

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10
Q

glucose + glucose = ?

A

maltose

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11
Q

glucose + galactose = ?

A

lactose

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12
Q

glucose + fructose = ?

A

sucrose

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13
Q

dissacharide

A

quick burst of short lived energy

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14
Q

polysaccharides

A

energy storing, for day or two

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15
Q

starch

A

plants, stored in plastids

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16
Q

glycogen

A

animals, stored in muscles and liver

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17
Q

cellulose

A

found in plant cell wall (leaves), herbivores

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18
Q

chitin

A

more complex than cellulose, found in insects, spider, crab

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19
Q

lipids

A

energy storage and barriers

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20
Q

what is the monomer of lipids?

A

fatty acids

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21
Q

glycerol

A

alcohol with 3 C’s and OH group

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22
Q

hydrocarbon chain

A

nonpolar, lots of energy stored

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23
Q

lipids can store two times the energy as _____?

A

carbs

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24
Q

saturated fat

A

from animals, solid at room temperature, no C=C

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25
Q

unsaturated fat

A

from plants, liquids or oils, one or more C=C

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26
Q

functions of lipids, specifically fats

A

cushioning around organs, insulation (blubber)

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27
Q

phospholipid bilayer

A

heads - polar, hydrophilic
tails - nonpolar, hydrophobic

28
Q

steroids

A

made of various functional groups

29
Q

what is the backbone to steroids?

A

cholesterol

30
Q

arteriosclerosis

A

build up plaque in arteries, heart attack

31
Q

polypeptide chains

A

proteins are a chain of amino acids linked together by peptide bonds

32
Q

what is the monomer of proteins?

A

amino acids

33
Q

R group: amino group

A

basic, positively charged

34
Q

R group: carboxyl group

A

acidic, negatively charged

35
Q

nonpolar R groups

A

no O, hydrophobic

36
Q

polar R groups

A

with -OH or just an = O, hydrophilic

37
Q

peptide bond formation

A

condensation rxn, amino end is designated at beginning and carboxyl end is designated at end

38
Q

protein conformation (shape)

A

normal, nature, typical shape

39
Q

primary structure

A

chain of amino acids in order, DNA recipe, mutation

40
Q

secondary structure

A

two types, caused by H bonding between amino acid and carboxyl groups:
helix - coil
pleated sheet - folded

41
Q

tertiary structure

A

different amino acids = different R groups
ionic bond - charged R groups
disulfide bridge - S-S
hydrogen bond - polar
van der waals - non polar

42
Q

quaternary structure

A

optional, 2 polypeptides join together to make protein, not all proteins have this level of structure

43
Q

denatured

A

change native confirmation (hair)

44
Q

sickle cell anemia

A

genetic change may cause protein shape change

45
Q

nucleic acids

A

central dogma

46
Q

DNA

A

stores and transmits coded info, determines amino acid sequences in proteins, nucleus (double stranded)

47
Q

RNA

A

takes DNA’s message out of the nucleus, forms ribosomes where proteins are made

48
Q

what is the monomer of a nucleic acid?

A

nucleotide

49
Q

ribose

50
Q

deoxyribose

51
Q

pyrimidines (1 ring)

A

cytosine
thymine (DNA only)
uracil (RNA only)

52
Q

purines (2 rings)

A

adenine
guanine

53
Q

polymer formation

A

direction matters, 3’ (OH) and 5’ (P)

54
Q

enzymes

A

proteins in the body that speed up a reaction

55
Q

catalyst

A

anything that speeds up a reaction

56
Q

activation energy

A

needed to start a reaction

57
Q

transition state

A

unstable point where the reactants have absorbed enough energy to break and store to rearrange

58
Q

substrate

A

reactant with enzyme

59
Q

active site

A

area of enzyme that binds to substrate

60
Q

induced fit

A

enzyme changes shape after binding, ex: handshake

61
Q

temp and pH

A

rate can increase or decrease, disrupts H- bonds and denatures proteins and enzymes

62
Q

cofactors

A

non protein helpers

63
Q

coenzymes

A

organic cofactors

64
Q

competitive inhibitiors

A

compete with substrate for active site

65
Q

noncompetitive inhibitors

A

molecule binds to a different area on enzyme and change its shape

66
Q

feedback inhibition

A

metabolic pathway is stopped when the product binds to the enzyme and inhibits activity

67
Q

localizing

A

specific enzymes for specific jobs

ap biology (9 decks)

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