chapter five part two Flashcards

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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
Q

hormone (communication) protein ex.

A

insulin causes tissues to take up glucose

26
Q

structural support protein ex.

A

keratin (hair), silk fibers

27
Q

enzymes

A

protein that regulates metabolism by acting as catalyst

28
Q

catalysts

A

chemical agents that selectively speed up chemical reactions w/o being consumed
- lowers energy of activation

29
Q

polypeptides

A

polymer of amino acids

30
Q

amino acids

A

building blocks of proteins

31
Q

how many different amino acids total?

A

20

32
Q

what does an amino acids consist of?

A
  • amino group
  • carboxyl group
  • hydrogen atom
  • variable group (R)
    all attached to C
33
Q

4 types of amino acids

A
  1. nonpolar
  2. polar
  3. asidic
  4. basic
34
Q

nonpolar AA

A

hydrophobic side chain

35
Q

polar AA

A

hydrophilic side chain

36
Q

acidic AA

A

negative side chain

37
Q

basic AA

A

positive side chain

38
Q

what are amino acids held together by?

A

peptide bonds
- made via dehydration reaction

39
Q

4 levels of protein structure

A

primary, secondary, tertiary, quaternary

40
Q

primary protein structure

A

linear chain of amino acids held together by peptide bonds

41
Q

secondary protein structure

A

regions stabilized by hydrogen bonds between atoms of polypeptide backbone
- alpha helix
- beta pleated sheets

42
Q

alpha helix

A

coil held together by H-bonding between every 4th AA

43
Q

beta pleated sheet

A

2+ segments of polypeptide chain connected by H-bonds
- core of globular proteins

44
Q

tertiary protein structure

A

3D shape stabilized by interactions between side chains
- hydrophobic interactions
- hydrogen bonds
- disulfide bridges

45
Q

hydrophobic interactions in tertiary structure

A

AA w/ hydrophobic side chains usually end up in clusters at core or protein out of contact w/ water

46
Q

disulfide bonds in tertiary structure

A

covalent bonds where 2 cysteine monomer (w/ sulfhydryl groups) are brought close together

47
Q

quaternary protein structure

A

when protein consists of 2+ polypeptide chains
- collagen
- hemoglobin (globular protein)

48
Q

denaturation

A

breakdown of protein shape

49
Q

causes of denaturation

A

pH, salt concentration, high temperature, chemicals that break H-bonds

50
Q

chaperonins

A

assist new proteins to fold/assemble into native shape

51
Q
A