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lecture 3b&4 Flashcards

1
Q

what is the t test used for*

A

to test for the significant difference between the means of two groups

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2
Q

when do you use the unpaired t test*

A

when comparing independent samples (from different individuals)

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3
Q

when do you not use the unpaired t test*

A

data comes from the same individual before and after
less or more than two groups
no averages

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4
Q

11 steps for t test*

A
  1. state the null and alternate hypotheses
  2. list the data of the control and experimental groups
  3. record the number of replicates for each group
  4. calculate the mean of each group
  5. calculate the variance of each group
  6. calculate the standard deviation
  7. calculate the t value
  8. choose a significant value (0.05)
  9. figure out if you should do a one tailed or two tailed test
  10. find the critical t value using the table
  11. compare both t values
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5
Q

what are degrees of freedom*

A

number of categories or classes minus 1
opportunity for change

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6
Q

what is the formula for df*

A

df = (n1 - 1) + (n2 - 1)

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7
Q

what type of hypothesis is one tailed*

A

directional

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8
Q

what type of hypothesis is a two tailed hypothesis*

A

non directional

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9
Q

all living things contain

A

carbohydrates, lipids, proteins and nucleic acids

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10
Q

organic compounds contain

A

carbon (carbon backbone)

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11
Q

properties of an organic molecule depend on

A

arrangement of the carbon skeleton (straight, branched, rings with long or short bonds)
functional groups (give molecule distinct chemical properties)

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12
Q

single unit of molecules

A

monomer

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13
Q

chain of monomers

A

polymer

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14
Q

how do you build polymers

A

dehydration synthesis where water is released which forms a new bond

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15
Q

what is hydrolysis

A

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

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16
Q

what is a carbohydrate

A

sugar

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17
Q

how are carbohydrates stored in humans

A

glycogen

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18
Q

how are carbohydrates stored in plants

A

starch

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19
Q

what are carbohydrates used for

A

broken down for cellular respiration
short term energy reserves in muscles
structure (cellulose)

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20
Q

carbs are found in which ratio

A

CH^2O= 1:2:1

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21
Q

monomers are which type of carbs

A

simple sugar

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22
Q

polymers are which type of carb

A

complex sugars

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23
Q

what is a monosaccharide

A

monomer of carbohydrates

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24
Q

types of monosaccharides

A

glucose, galactose, fructose

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25
Q

what are disaccharides

A

two linked monosaccharides

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26
Q

what is sucrose

A

glucose plus fructose

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27
Q

glucose plus galactose

A

lactose

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28
Q

glucose plus glucose

A

maltose

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29
Q

what are polysaccharides

A

polymers of monosaccharides

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30
Q

types of polysaccharides

A

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

31
Q

what is the main feature of lipids

A

they are hydrophobic

32
Q

function of neutral fats

A

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

33
Q

structure of neutral fats

A

1 molecule of glycerol
1-3 molecules of fatty acids

34
Q

3 molecules of fatty acids is called

A

triglyceride

35
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 do have double bonds
saturated fatty acids are then easier to stack since there is no bend in the chain

36
Q

differences between cis unsaturated and trans unsaturated fatty acids

A

more bend for cis

37
Q

function of phospholipids

A

major constituent of cell membranes

38
Q

structure of phospholipids

A

2 molecules of fatty acids
1 glycerol molecule
1 phosphate molecule

39
Q

what is an amphipathic molecule

A

a molecule that has a side which is hydrophilic and a side that is hydrophobic (phospholipid)

40
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)

41
Q

how does the phospholipid assemble

A

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

42
Q

what are the functions of steroids

A

cell membrane (cholesterol)
vitamins
hormones

43
Q

structure of steroids

A

made from sterol (multiple rings of carbon)

44
Q

what do proteins do

A

pretty much everything (transport, enzymes, antibodies,storage, etc)

45
Q

proteins are made from

A

amino acids

46
Q

what is a polypeptide

A

a polymer of amino acids

47
Q

structure of amino acid

A

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

48
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)

49
Q

is the polypeptide polar

A

yes

50
Q

why is the shape of a protein important

A

the shape of the protein determines its function

51
Q

how many levels of structure are there in proteins

A
  1. primary
  2. secondary
  3. tertiary
  4. quaternary
52
Q

what is the primary structure of proteins

A

the specific and unique sequence of amino acids that make up a polypeptide

53
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)

54
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

55
Q

what is the secondary structure of proteins

A

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

56
Q

what causes the folding/coiling of proteins

A

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

57
Q

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

A

coil
bond occurs every fourth amino acid

58
Q

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

59
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

60
Q

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

61
Q

how is the distance between pleats decided in beta p.s.

A

the strong covalent bonds of the polypeptide backbone

62
Q

what is the tertiary structure of a protein

A

the forces holding a singular polypeptide together

63
Q

what determines the the 3D structure of a single polypeptide

A
  1. hydrogen bonds
  2. ionic bonds
  3. hydrophobic interactions
  4. covalent/disulphide bonds
64
Q

what are ionic bonds

A

results from ions/ plus minus charged particles

65
Q

what are hydrophobic interactions

A

hydrophobic molecules interacting with each other

66
Q

what is a disulphide bond

A

bond between sulphide groups on amino acids (covalent bond)

67
Q

what is the quaternary structure

A

the fusion of two or more polypeptide

68
Q

how is the quaternary structure formed

A

by the interactions among polypeptide chains
has the same types of bonds as the tertiary structure

69
Q

what is a monomeric protein

A

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

70
Q

what is an oligomeric protein

A

protein made of two or more polypeptide chains

71
Q

what is denaturation

A

when a protein breaks down by unravelling or changing shape (permanent or temporary)

72
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.)

73
Q

what can cause denaturation

A

heat and alcohol

74
Q

ribosomes characteristics (3)

A

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

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