chapter five part two Flashcards

1
Q

what are lipids

A

hydrophobic molecules that don’t mix with water

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2
Q

element composition of lipids

A

C,H, and some O
- mostly hydrocarbon/nonpolar regions

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3
Q

composition of fats

A

glycerol molecule, 3 fatty acids

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4
Q

covalent bonds in nucleic acids

A

phosphodiester

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5
Q

covalent bond in lipids

A

ester linkages between glycerol and fatty acids

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6
Q

fatty acids

A

have long carbon skeleton (16-18) C at one end is part of carboxyl group
- contains carboxyl and methyl groups

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7
Q

traicylglycerol
(triglyceride)

A

fat molecule w/ 3 fatty acids
- “cyl” = fatty acid

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8
Q

saturated fats

A

have all the hydrogen it can hold

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9
Q

unsaturated fats

A

has one or more double bonds
- creates kink in tail
- liquid at room temperature

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10
Q

uses of fats

A

energy storage, cushions vital organs

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11
Q

phospholipid composition

A

glycerol molecule, 2 fatty acids, 3rd hydroxyl group

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12
Q

what are phospholipids a major component of?

A

cell membranes
- hydrophobic tail
- hydrophilic head

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13
Q

steroids

A

lipids characterized by 4 fused rings in carbon skeleton and a functional group

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14
Q

cholesterol

A

precursor of many steroids

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15
Q

what is cholesterol good for?

A

component of animal cell membranes, synthesizes hormones

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16
Q

proteins

A

biologically functional molecule made up of polypeptides and chains of amino acids

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17
Q

how abundant are proteins in a cell?

A

50% of dry mass

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18
Q

functions of proteins
(STERCDHS)

A
  1. storage
  2. transport
  3. enzymatic
  4. receptor
  5. contractile
  6. defense
  7. hormone (communication)
  8. structural support
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19
Q

storage protein ex.

A

casein protein of milk stores amino acids

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20
Q

transport protein ex.

A

hemoglobin transports oxygen

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21
Q

enzymatic protein ex.

A

digestive enzymes catalyze hydrolysis in bonds of food

22
Q

receptor protein ex.

A

neuromuscular junction

23
Q

contractile protein ex.

A

actin and myosin responsible for contraction of muscles

24
Q

defense protein ex.

A

protection against disease, antibodies help destroy viruses

25
hormone (communication) protein ex.
insulin causes tissues to take up glucose
26
structural support protein ex.
keratin (hair), silk fibers
27
enzymes
protein that regulates metabolism by acting as catalyst
28
catalysts
chemical agents that selectively speed up chemical reactions w/o being consumed - lowers energy of activation
29
polypeptides
polymer of amino acids
30
amino acids
building blocks of proteins
31
how many different amino acids total?
20
32
what does an amino acids consist of?
- amino group - carboxyl group - hydrogen atom - variable group (R) all attached to C
33
4 types of amino acids
1. nonpolar 2. polar 3. asidic 4. basic
34
nonpolar AA
hydrophobic side chain
35
polar AA
hydrophilic side chain
36
acidic AA
negative side chain
37
basic AA
positive side chain
38
what are amino acids held together by?
peptide bonds - made via dehydration reaction
39
4 levels of protein structure
primary, secondary, tertiary, quaternary
40
primary protein structure
linear chain of amino acids held together by peptide bonds
41
secondary protein structure
regions stabilized by hydrogen bonds between atoms of polypeptide backbone - alpha helix - beta pleated sheets
42
alpha helix
coil held together by H-bonding between every 4th AA
43
beta pleated sheet
2+ segments of polypeptide chain connected by H-bonds - core of globular proteins
44
tertiary protein structure
3D shape stabilized by interactions between side chains - hydrophobic interactions - hydrogen bonds - disulfide bridges
45
hydrophobic interactions in tertiary structure
AA w/ hydrophobic side chains usually end up in clusters at core or protein out of contact w/ water
46
disulfide bonds in tertiary structure
covalent bonds where 2 cysteine monomer (w/ sulfhydryl groups) are brought close together
47
quaternary protein structure
when protein consists of 2+ polypeptide chains - collagen - hemoglobin (globular protein)
48
denaturation
breakdown of protein shape
49
causes of denaturation
pH, salt concentration, high temperature, chemicals that break H-bonds
50
chaperonins
assist new proteins to fold/assemble into native shape
51