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Biology I > Macromolecules > Flashcards

Macromolecules Flashcards

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1
Q

what do all living things contain

A

proteins, carbs, lipids

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2
Q

what do organic compounds contain

A

carbon (carbon backbone), can form long chains and combine with other atoms (H, O, N, P, S)

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3
Q

what do properties of an organic molecule depend on

A
  1. arrangement of the carbon skeleton (straight, branched, rings with long or short bonds)
  2. functional groups are attached to carbon skeleton (give molecule distinct chemical properties)
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4
Q

what are 7 functional groups

A

aldehyde
carbonyl
carboxyl
phosphate
hydroxyl
sulfhydryl
amino

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5
Q

Small change in form causes…

A

a change in function

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6
Q

what is a single unit of molecules

A

monomer

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7
Q

what is a chain or ring of monomers

A

polymer

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8
Q

how do you build polymers

A

dehydration synthesis where water is released which forms a new bond, enzyme acts as a catalyst

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9
Q

what is hydrolysis

A

when water is added and a bond is broken in the polymer chain

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10
Q

what are the four classes of biological molecules

A

carbs, lipids, proteins, nucleic acids

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11
Q

what is a carbohydrate

A

sugar, source of energy

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12
Q

what are carbohydrates used for

A

-broken down for cellular respiration
-short term energy reserves in muscles and liver in animals
-structure (cellulose)

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13
Q

how are carbohydrates stored in humans

A

glycogen

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14
Q

how are carbohydrates stored in plants

A

starch

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15
Q

what is the ratio for carbohydrates

A

CH^2O = 1:2:!

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16
Q

what type of sugars are monomers

A

simple sugars

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17
Q

what type of sugars are polymers

A

complex sugars

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18
Q

what is a monosaccharide

A

monomer of carbohydrates

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19
Q

what are types of monosaccharides

A

glucose, galactose, fructose

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20
Q

what are disaccharides

A

two linked monosaccharides

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21
Q

what is sucrose

A

glucose + fructose (table sugar)

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22
Q

what is lactose

A

glucose + galactose (milk sugar)

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23
Q

what is maltose

A

glucose + glucose (brewing sugar)

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24
Q

what are polysaccharides

A

polymers of monosaccharides

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25
Q

what are types of polysaccharides

A

storage and structural carbohydrates (starch, glycogen & cellulose, chitin)

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26
Q

what is special about herbivores

A

they eat plants that contain cellulose but do not produce enzymes to break them down. the bacteria in their digestive system breaks it down

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27
Q

what is special about lipids

A

they are hydrophobic (do not sdissolve in water)

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28
Q

what are 3 main types of lipids

A

-neutral fats
-phospholipids
-steroids

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29
Q

what are the functions of neutral fats

A

-long term energy reserve in fat tissue
-maintain body temperature through insulation
-protect vital organs
-buoyancy

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30
Q

what is the sustructure of fat

A

1 molecule of glycerol
1-3 molecules of fatty acids

31
Q

what are 3 molecules of fatty acids is called

A

triglyceride

32
Q

what is the difference between saturated and unsaturated fatty acids

A

saturated fatty acids have no double bonds between the carbon atoms while unsaturated fatty acids have double bonds
-saturated fatty acids are then easier to stack since there is no bend in the chain

33
Q

what is the difference between cis unsaturated and trans unsaturated fatty acids

A

trans is less of a bend and cis is more of a bend

34
Q

what is the function of phospholipids

A

major constituent of cell membranes

35
Q

what is the structure of phospholipids

A

2 molecules of fatty acids
1 glycerol molecule
1 phosphate molecule

36
Q

what is an amphipathic molecule

A

a molecule that has a side which is hydrophilic and a side that is hydrophobic (phospholipid) basically can interact with both fats and water

37
Q

which part of the phospholipid is attracted/repelled by water

A

the head is attracted to water (hydrophilic)
the tail is repelled by water (hydrophobic)

38
Q

how does the phospholipid assemble

A

into a double layer that has the hydrophobic portions facing each other

39
Q

what are the functions of steroids

A

cell membrane (cholesterol)
vitamins
hormones

40
Q

what is the structure of steroids

A

made from sterol (multiple rings of carbon)

41
Q

what do proteins do

A

transport, enzymes (break down and build), antibodies, storage

42
Q

what are proteins made of

A

amino acids (the polypeptides of protein)

43
Q

what is a polypeptide

A

a polymer of amino acids

44
Q

what is a protein

A

1 or more functional polypeptides folded/coiled into a specific shape

45
Q

what is the structure of an amino acid

A

2 functional groups (amino and carboxyl)
1 variable group (R)
a hydrogen

46
Q

how do you link amino acids to make a polypeptide and where

A

dehydration synthesis/condensation reaction
link at the n-terminus and the c-terminus (amino and carboxyl ends)

47
Q

is the polypeptide polar

A

yes

48
Q

why is the shape of a protein important

A

the shape of the protein determines its function

49
Q

how many levels of structure are there in proteins

A

primary
secondary
tertiary
quaternary

50
Q

what is the primary structure of proteins

A

the specific and unique sequence of amino acids that make up a polypeptide
- strong covalent bonding

51
Q

how is the unique sequence of a.a. determined in the primary structure

A

by the nucleotide sequence of the gene that encodes the protein (genetically determined)

52
Q

what happens to the protein if an amino acid get switched

A

it will change the form of the protein which will affect how it performs its function

53
Q

what is the secondary structure of proteins

A

the folding and coiling of a sequence of amino acids within a polypeptide

54
Q

what causes the folding/coiling of proteins

A

hydrogen bonds between the amino and carboxyl groups in the polypeptide’s backbone

55
Q

what is an alpha helix and where do the h-bonds occur

A

coil
bond occurs every fourth amino acid

56
Q

what is a beta pleaded sheet and where do h-bonds occur

A

pleated sheet of polypeptide lying parallel
h-bonds between amino and carboxyl group

56
Q

what are alpha helix characteristics

A

common in fibrous proteins (hair, skin, nails)
h-bonds are strong when there are many bonds (weak individually)
able to stretch and reform

57
Q

what are beta pleaded sheet characteristics

A

make up core of globular proteins and some fibrous proteins like fibroin (spider silk)
strong and flexible but not elastic
can twist
very strong

58
Q

how is the distance between pleats decided in beta pleaded sheets

A

the strong covalent bonds of the polypeptide backbone

59
Q

what is the tertiary structure of a protein

A

the forces holding a singular polypeptide together

60
Q

what determines the the 3D structure of a single polypeptide

A

hydrogen bonds
ionic bonds
hydrophobic interactions
covalent/disulphide bonds

61
Q

what are ionic bonds

A

results from ions/ plus minus charged particles

62
Q

what are hydrophobic interactions

A

non-water soluble molecules interacting with each other

63
Q

what is a covalent/disulphide bond

A

equal sharing of electrons between sulfide groups on a.a.

64
Q

what is the quaternary structure

A

the fusion of two or more polypeptide

65
Q

how is the quaternary structure formed

A

by the interactions among polypeptide chains
has the same types of bonds as the tertiary structure
ex: hemoglobin and collagen

66
Q

what is a monomeric protein

A

protein made of a singular polypeptide chain (no quaternary structure)

67
Q

what is an oligomeric protein

A

protein made of two or more polypeptide chains

68
Q

what is denaturation

A

when a protein breaks down by unravelling or changing shape (permanent or temporary)
ex: egg frying

69
Q

what happens during denaturation

A

disruption or destruction of secondary and tertiary structures
disrupts alpha h. and beta p.s so becomes a random shape
primary sequence remains due to the reaction not being strong enough to break the peptide bonds (except at very high temp.)

70
Q

what can cause denaturation

A

heat and alcohol

71
Q

what are 3 ribosome characteristics

A

displays quaternary structure
uses RNA to make other proteins
made in nucleolus

72
Q

what are 3 kind of mutations

A

neutral
detrimental
beneficial

Biology I (11 decks)

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