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bio module 2 > proteins > Flashcards

proteins Flashcards

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1
Q

elements in proteins?

A

C H O & N

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2
Q

“peptide” definition

A

polymers made of amino acid molecules (monomers) with specific biological functions

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3
Q

amino acid structure?

A

centre carbon
- R group
- amine group (NH2)
- H
- carboxyl group (COOH)

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4
Q

what makes amino acids different?

A

different R groups

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5
Q

how many amino acids are commonly found in cells?

A

20

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6
Q

how many amino acids are essential & non-essential & conditionally essential?

A

essential = 9
non-essential = 5
conditionally essential = 6

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7
Q

what are conditionally essential amino acid?

A

only needed in growing children

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8
Q

when do amino acids join?

A

when the amine and carboxylic acid groups connected to central carbon react

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9
Q

how do amino acids react with each other?

A

peptide bond formed + water produced

when hydroxyl of one amino acid reacts w hydrogen of another

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10
Q

what type of reaction is amino acid synthesis?

A

condensation reaction

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11
Q

what bond forms between amino acids?

A

peptide bonds

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12
Q

polymer of amino acids?

A

polypeptide

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13
Q

monomer of polypeptides?

A

amino acids

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14
Q

enzyme catalysing polypeptide synthesis?

A

peptidyl transferase (ribosomes)

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15
Q

where is the enzyme for polypeptide synthesis found?

A

peptidyl transferase in the ribosomes

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16
Q

how do amino acid chains fold into proteins?

A

bonds formed by amino acid R groups

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17
Q

what do different amino acids do for protein structure?

A

diff amino acids fold polypeptide chains into different proteins w/ different shapes

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18
Q

“primary protein structure”

A

the sequence in which amino acids are joined

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19
Q

what bonds are involved in primary protein structure?

A
  • peptide bonds
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20
Q

“secondary protein structure”

A

O H & N of basic repeating amino acid structures interact, forming H bonds between amino acids = a helix or b pleated sheet structures

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21
Q

a helix structure

A

hydrogen bonds within amino acid chain pull into coil shape

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22
Q

b pleated sheet

A

polypeptide chains lie parallel to each other joined by hydrogen bonds = sheet like structures

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23
Q

what bonds are involved in secondary structure?

A

hydrogen bonds (+ peptide primary)

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24
Q

“tertiary protein structure”

A

how the folding of secondary structure into protein brings R groups close via disulfide bridges, ionic bonds, hydrogen bonds & hydrophobic hydrophilic interactions to form a 3D structure

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25
Q

what bonds are involved in tertiary protein structure?

A
  • h bonds (weakest)
  • ionic bonds (between opp charged R groups)
  • disulfide bridges (covalent + strongest but only between sulfur containing R groups)
  • hydrophobic philic (weak polar non-polar interactions)
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26
Q

tertiary hydrogen bonds?

A

weakest bonds

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27
Q

tertiary ionic bonds?

A

between opp charged R groups

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28
Q

tertiary sulfide bridges?

A

covalent + strongest bonds between sulfur containg R groups

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29
Q

tertiary hydrophobic hydrophilic interactions?

A

weak interactions between polar & non-polar R groups

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30
Q

“quaternary protein structure”

A

result of association of 2+ individual proteins (subunits)

aka tertiary structure bonds between proteins not R groups

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31
Q

“subunits”

A

individual proteins

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32
Q

how many subunits does insulin have?

A

2 identical subunits

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33
Q

how many subunits does haemoglobin have?

A

2 different sets of 2 identical subunits

34
Q

where are protein hydrophilic groups?

A

outside (cytoplasm)

35
Q

where are protein hydrophobic groups?

A

inside (away from cytoplasm water)

36
Q

reaction breaking peptides down?

A

hydrolysis

37
Q

“dipeptide”

A

product of 2 amino acids joined (monomers)

38
Q

“tripeptide”

A

product of 3 amino acids joined together (monomers)

39
Q

“polypeptide”

A

polymer produced when many amino acids (monomers) are joined together

40
Q

“amphoteric” (amino acids are [] )

A

molecule that acts as base and acid

41
Q

“amorphous regions”

A

regions without a helixes or b pleated sheets in secondary structure

42
Q

“globular proteins”

A

compact, water soluble molecules with chemical properties

43
Q

globular protein characteristics

A
  • compact
  • water soluble
  • spherical
44
Q

why are globular proteins water soluble?

A

tertiary structure where hydrophobic R groups inside + hydrophilic R groups outside

45
Q

why is globular protein solubility important?

A

regulating processes
- eg. chemical reactions
- immunity
- muscle contractions etc

46
Q

“insulin” definition

A

globular protein hormone involved in regulating blood glucose levels

47
Q

why do hormones need to be soluble?

A

transported in blood stream

48
Q

how do hormones need precise shapes?

A

need to fit specific receptors on cell surface membranes for effect

49
Q

“conjugated protein” definition

A

globular protein contains a non-protein component (prosthetic group)

50
Q

“prosthetic group”

A

non-protein component

51
Q

“simple protein” definition

A

protein not containing a prosthetic group

52
Q

are lipids / carbohydrates prosthetic groups?

A

yes

53
Q

what are lipoproteins?

A

lipid (pros group) + protein

54
Q

what are glycoproteins?

A

carbohydrate (pros group) + protein

55
Q

what can form prosthetic groups?

A
  • lipids
  • carbs
  • metal ions
  • molecules derived from vitamins

- haem groups containing Fe2+

56
Q

what molecules have haem groups?

A
  • haemoglobin
  • catalase
57
Q

what is haemoglobin?

A

red, oxygen-carrying pigment found in RBCs

58
Q

what is the structure of haemoglobin?

A

quaternary protein of four polypeptides
- 2 alpha subunits
- 2 beta subunits

59
Q

how many subunits in haemoglobin and what do they contain?

A

2 alpha + 2 beta - each has a prosthetic haem group

60
Q

what allows haemoglobin to take up and transfer oxygen?

A

Fe2+ ions in haem group bind reversible with O2 molecules = carried for transportation from lungs to cells

61
Q

“catalase”

A

enzyme containing 4 haem prosethic groups that catalyses breaking down in metabolism

62
Q

“enzyme” definition

A

catalyse and speed up rate of reaction by introducing alternate reaction pathway without being used up themselves specific to a reaction

63
Q

structure of catalase?

A

quaternary protein with 4 prosthetic haem groups

64
Q

reason for haem groups in catalase?

A

4 haem groups - Fe2+ ions allow catalase to interact with hydrogen peroxide and speed up break down

65
Q

what is hydrogen peroxide?

A

byproduct of metabolism damaging to cells and cell components if allowed to accumulate

66
Q

“fibrous proteins”

A

formed from long, insoluble molecules due to high proportion of hydrophobic R group in primary structure proteins

67
Q

fibrous protein structure?

A
  • limited range of amino acids
  • small R groups
  • repetitive amino acid primary structure sequence = organised structure
  • strong long molecules NOT FOLDED INTO 3D SHAPES like globular proteins
68
Q

why do fibrous proteins have an organised structure?

A

repetitive primary structure amino acid sequence

69
Q

fibrous protein examples? where are they found?

A
  • keratin (hair skin nails)
  • elastin (blood vessels alveoli in lung)
  • collagen (muscles bones tendons ligaments)
70
Q

“keratin”

A

fibrous protein in hair, skin and nails with large proportion of sulfur containing amino acids

71
Q

keratin characteristics?

A
  • strong
  • inflexible
  • insoluble
72
Q

what does keratin have its characteristics?

A

disulfide bonds = strong, inflexible, insoluble

less bonds (hair) = more flexible

73
Q

keratin bonds?

A

disulfide bonds - more (nails) = less flexible than less (hair) = flexible

74
Q

what is the smell when hair / skin is burnt?

A

burning of sulfur

75
Q

“elastin”

A

fibrous protein found in elastic fibres allowing for stretching and returning to original size

76
Q

where are elastic fibres found?

A

blood vessel walls & alveoli of lungs

77
Q

elastin structure?

A

quaternary protein made of tropoelastin (stretchy molecules)

78
Q

benefits of elastin?

A

allow structures to expand flexibly and return to original shape

79
Q

“collagen”

A

fibrous protein connective tissue found in skin, tendons, ligaments, nervous system

80
Q

collagen characteristics?

A
  • strong
  • flexible
81
Q

why are collagen’s characteristics like that?

A

Wound of 3 polypeptides wound together in long, rope-like structure

bio module 2 (7 decks)

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