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cegep biology > lecture 4 > Flashcards

lecture 4 Flashcards

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1
Q

all living things contain

A

carbohydrates, lipids, proteins and nucleic acids

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2
Q

organic compounds contain

A

carbon (carbon backbone)

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3
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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4
Q

single unit of molecule

A

monomer

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5
Q

chain of monomers

A

polymer

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6
Q

how do you build polymers

A

dehydration synthesis where water is released which forms a new bond

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7
Q

what is hydrolysis

A

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

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8
Q

what is a carbohydrate

A

sugar

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9
Q

how are carbohydrates stored in humans

A

glycogen

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10
Q

how are carbohydrates stored in plants

A

starch

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11
Q

what are carbohydrates used for

A

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

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12
Q

carbs are found in which ratio

A

CH^2O= 1:2:1

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13
Q

monomers are which type of carbs

A

simple sugars

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14
Q

polymers are which type of carb

A

complex sugars

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15
Q

what is a monosaccharide

A

monomer of carbohydrates

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16
Q

types of monosaccharides

A

glucose, galactose, fructose

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17
Q

what are disaccharides

A

two linked monosaccharides

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18
Q

what is sucrose

A

glucose plus fructose

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19
Q

glucose plus galactose

A

lactose

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20
Q

glucose plus glucose

A

maltose

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21
Q

what are polysaccharides

A

polymers of monosaccharides

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22
Q

types of polysaccharides

A

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

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23
Q

what is the main feature of lipids

A

they are hydrophobic

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24
Q

function of neutral fats

A

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

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25
structure of neutral fats
1 molecule of glycerol 1-3 molecules of fatty acids
26
3 molecules of fatty acids is called
triglyceride
27
what is the difference between saturated and unsaturated fatty acids
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
28
differences between cis unsaturated and trans unsaturated fatty acids
more bend for cis
29
function of phospholipids
major constituent of cell membranes
30
structure of phospholipids
2 molecules of fatty acids 1 glycerol molecule 1 phosphate molecule
31
what is an amphipathic molecule
a molecule that has a side which is hydrophilic and a side that is hydrophobic (phospholipid)
32
which part of the phospholipid is attracted/repelled by water
the head is attracted to water (hydrophilic) the tail is repelled by water (hydrophobic)
33
how does the phospholipid assemble
into a double layer that has the hydrophobic portions facing each other
34
what are the functions of steroids
cell membrane (cholesterol) vitamins hormones
35
structure of steroids
made from sterol (multiple rings of carbon)
36
what do proteins do
pretty much everything (transport, enzymes, antibodies,storage, etc)
37
proteins are made from
amino acids
38
what is a polypeptide
a polymer of amino acids
39
structure of amino acid
2 functional groups (amino and carboxyl) 1 variable group (R) a hydrogen all around a carbon
40
how do you link amino acids to make a polypeptide and where
dehydration synthesis/condensation reaction link at the n-terminus and the c-terminus (amino and carboxyl ends)
41
is the polypeptide polar
yes
42
why is the shape of a protein important
the shape of the protein determines its function
43
how many levels of structure are there in proteins
1. primary 2. secondary 3. tertiary 4. quaternary
44
what is the primary structure of proteins
the specific and unique sequence of amino acids that make up a polypeptide
45
how is the unique sequence of a.a. determined in the primary structure
by the nucleotide sequence of the gene that encodes the protein (genetically determined)
46
what happens to the protein if an amino acid get switched
it will change the form of the protein which will affect how it performs its function
47
what is the secondary structure of proteins
the folding and coiling of a sequence of amino acids within a polypeptide
48
what causes the folding/coiling of proteins
hydrogen bonds between the amino and carboxyl groups in the polypeptide’s backbone
49
what is an alpha helix and where do the h-bonds occur
coil bond occurs every fourth amino acid
50
alpha helix characteristics
common in fibrous proteins (hair, skin, nails) h-bonds are strong when there are many bonds (weak individually) able to stretch
51
what is a beta pleaded sheet and where do h-bonds occur
pleated sheet of polypeptide lying parallel h-bonds between amino and carboxyl group
52
beta pleaded sheet characteristics
make up core of globular proteins and some fibrous proteins like fibroin (spider silk) strong and flexible but not elastic can twist
53
how is the distance between pleats decided in beta p.s.
the strong covalent bonds of the polypeptide backbone
54
what is the tertiary structure of a protein
the forces holding a singular polypeptide together
55
what determines the the 3D structure of a single polypeptide
1. hydrogen bonds 2. ionic bonds 3. hydrophobic interactions 4. covalent/disulphide bonds
56
what are ionic bonds
results from ions/ plus minus charged particles
57
what are hydrophobic interactions
hydrophobic molecules interacting with each other
58
what is a disulphide bond
bond between sulphide groups on amino acids (covalent bond)
59
what is the quaternary structure
the fusion of two or more polypeptide
60
how is the quaternary structure formed
by the interactions among polypeptide chains has the same types of bonds as the tertiary structure
61
what is a monomeric protein
protein made of a singular polypeptide chain (no quaternary structure)
62
what is an oligomeric protein
protein made of two or more polypeptide chains
63
what is denaturation
when a protein breaks down by unravelling or changing shape (permanent or temporary)
64
what happens during denaturation
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.)
65
what can cause denaturation
heat and alcohol
66
ribosomes characteristics (3)
displays quaternary structure uses RNA to make other proteins made in nucleolus

cegep biology (11 decks)

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